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9i19

Iron loaded human H-chain ferritin D131N mutant 5 minute oxygen soak

Method: X-RAY DIFFRACTION Dmax: 72.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Ferritin heavy chain

Homo sapiens

UniProt P02794

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein homooligomer Homooligomer Protein × 24 PDB declaration: monomeric（1） Count mismatch; review required Chain A； UniProt 1–183 Not recorded FE FE (III) ION × 72 MG MAGNESIUM ION × 96 CL CHLORIDE ION × 96 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；0.1 M Bicine 2 M Magnesium chloride 0.1 M Sodium chloride 60 mM Ferrous chloride 3 mM Sodium chloride Resolution 1.63 Å R-free 0.192

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 9I19 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1FHA SOLVING THE STRUCTURE OF HUMAN H FERRITIN BY GENETICALLY ENGINEERING INTERMOLECULAR CRYSTAL CONTACTS Deposited 1990-12-20 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Not recorded FE FE (III) ION × 24 CA CALCIUM ION × 48 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å
21HO Crystal strucrue of HuHF-C2-MEO complex Deposited 2025-12-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.40 Å R-free 0.241
21KV Crystal strucrue of HuHF-C2-DAC complex Deposited 2025-12-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.202
21KW Crystal strucrue of HuHF-C2-SEM complex Deposited 2025-12-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.200
21LE Crystal strucrue of HuHF-C2-CAR complex Deposited 2025-12-17 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.187
28JY Iron loaded E61A human H-chain ferritin, anaerobic Deposited 2026-02-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å R-free 0.198
28JZ Iron loaded E61A human H-chain ferritin, 1 hour oxygen soak Deposited 2026-02-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.41 Å R-free 0.239
28KA Iron loaded human H-chain ferritin, anaerobic Deposited 2026-02-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.11 Å R-free 0.191
28KB Iron loaded human H-chain ferritin, 3 hour oxygen soak Deposited 2026-02-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.83 Å R-free 0.228
28KC Iron loaded human H-chain ferritin, 2 minute oxygen soak Deposited 2026-02-04 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.94 Å R-free 0.192
28LZ Iron loaded human H-chain ferritin, 20 minute oxygen soak Deposited 2026-02-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.94 Å R-free 0.195
2CEI Recombinant human H ferritin, K86Q mutant, soaked with Zn Deposited 2006-02-07 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES ZN ZINC ION × 192 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；HANGING DROP. RESERVOIR: MPD 21%, CACL2 5.7 MM, HEPES 50 MM PH 7.5 DROP: 2 UL PROTEIN (4.5 MG/ML) AND 1 UL RESERVOIR
Resolution 1.80 Å R-free 0.192
2CHI Recombinant human H ferritin, K86Q and E27D mutant Deposited 2006-03-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES CA CALCIUM ION × 72 ZN ZINC ION × 48 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；HANGING DROP. RESERVOIR: MPD 5%, CACL2 4.7 MM, HEPES 50 MM PH 7.5 DROP: 1 UL PROTEIN (27MG/ML) AND 1 UL RESERVOIR
Resolution 1.60 Å R-free 0.193
2CIH Recombinant human H ferritin, K86Q and E27D mutant, soaked with Zn Deposited 2006-03-21 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES ZN ZINC ION × 216 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；HANGING DROP. RESERVOIR: MPD 5% CACL2 4.7 MM, HEPES 50 MM PH 7.5 DROP: 1 UL PROTEIN (27MG/ML) AND 1 UL RESERVOIR
Resolution 1.50 Å R-free 0.198
2CLU Recombinant human H ferritin, K86Q and E107D mutant Deposited 2006-05-02 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES CA CALCIUM ION × 48 ZN ZINC ION × 24 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP. RESERVOIR: MPD 5% CACL2 4.7 MM, TRIS 50 MM PH 8.5. DROP: 1 UL PROTEIN (22 MG/ML) AND 1 UL RESERVOIR
Resolution 2.10 Å R-free 0.246
2CN6 Recombinant human H ferritin, K86Q and E107D mutant, soaked with Zn ions Deposited 2006-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES ZN ZINC ION × 168 CA CALCIUM ION × 24 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP. RESERVOIR: MPD 5% CACL2 4.7 MM, TRIS 50 MM PH 8.5 DROP: 1 UL PROTEIN (22 MG/ML) AND 1 UL RESERVOIR
Resolution 2.20 Å R-free 0.230
2CN7 Recombinant human H ferritin, K86Q, E27D and E107D mutant Deposited 2006-05-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES CA CALCIUM ION × 72 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP. RESERVOIR: MPD 5.2%, CACL2 3.9 MM, TRIS 50MM PH 8.5. DROP: 1UL PROTEIN (24 MG/ML) AND 1 UL RESERVOIR
Resolution 1.75 Å R-free 0.204
2FHA HUMAN H CHAIN FERRITIN Deposited 1997-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：K86Q CA CALCIUM ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 0.08% CACL2 / 15% MPD IN 50 MM HEPES BUFFER PH 7.5
Resolution 1.90 Å
2IU2 Recombinant human H ferritin, K86Q, E27D and E107D mutant, soaked with Zn ions Deposited 2006-05-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–182（182 aa）
Mutation：YES ZN ZINC ION × 144 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；HANGING DROP. RESERVOIR : MPD 5.2%, CACL2 3.9 MM, TRIS 50 MM PH 8.5. DROP: 1UL PROTEIN (24 MG/ML) AND 1 UL RESERVOIR
Resolution 1.80 Å R-free 0.219
2Z6M Crystal structure of Human Ferritin H8 as biotemplate for noble metal nanoparticle synthesis Deposited 2007-08-04 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–177（176 aa） Fragment：residues 1-176
Chain B 2–177（176 aa） Fragment：residues 1-176
Chain C 2–177（176 aa） Fragment：residues 1-176
Chain D 2–177（176 aa） Fragment：residues 1-176
Chain E 2–177（176 aa） Fragment：residues 1-176
Chain F 2–177（176 aa） Fragment：residues 1-176
Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C ZN ZINC ION × 8 CA CALCIUM ION × 8 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；protein solution(11.0 mg/mL H8 in unbuffered 3.0mM NaN3), 2.5mL of precipitant buffer(0.1 M sodium acetate(pH 4.6), 20%(v/v) isopropanol, 0.2M CaCl2) , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.72 Å R-free 0.252
2Z6M Crystal structure of Human Ferritin H8 as biotemplate for noble metal nanoparticle synthesis Deposited 2007-08-04 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 2–177（176 aa） Fragment：residues 1-176
Chain H 2–177（176 aa） Fragment：residues 1-176
Chain I 2–177（176 aa） Fragment：residues 1-176
Chain J 2–177（176 aa） Fragment：residues 1-176
Chain K 2–177（176 aa） Fragment：residues 1-176
Chain L 2–177（176 aa） Fragment：residues 1-176
Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C ZN ZINC ION × 12 CA CALCIUM ION × 8 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；protein solution(11.0 mg/mL H8 in unbuffered 3.0mM NaN3), 2.5mL of precipitant buffer(0.1 M sodium acetate(pH 4.6), 20%(v/v) isopropanol, 0.2M CaCl2) , VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.72 Å R-free 0.252
3AJO Crystal structure of wild-type human ferritin H chain Deposited 2010-06-11 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded MG MAGNESIUM ION × 288 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0M magnesium chloride, 0.1M Bicine (pH 9.0), VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.52 Å R-free 0.183
3AJP Crystal structure of human H ferritin E140A mutant Deposited 2010-06-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E140A MG MAGNESIUM ION × 240 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0M magnesium chloride, 0.1M Bicine (pH 9.0), VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.218
3AJQ Crystal structure of human H ferritin E140Q mutant Deposited 2010-06-11 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E140Q MG MAGNESIUM ION × 264 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0M magnesium chloride, 0.1M Bicine (pH 9.0), VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.58 Å R-free 0.185
3ERZ Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. Mercury Ions on the Three-Fold Channel Deposited 2008-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 24 HG MERCURY (II) ION × 24 CA CALCIUM ION × 4 ZN ZINC ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；protein solution (11.0 mg/mL H8 in unbuffered 3.0MM NAN3), 2.5mL of precipitant buffer (0.1M sodium acetate (PH 4.6), 20%(v/v) isopropanol, 0.2M CaCl2), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. Soaking experiment performed with mercury ions using the mother liquor without calcium ions.
Resolution 3.06 Å R-free 0.256
3ERZ Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. Mercury Ions on the Three-Fold Channel Deposited 2008-10-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C Mutation：H13D, E64C, C90R, C102A, H105Q, E140C, K143C, E147C MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 20 HG MERCURY (II) ION × 24 CA CALCIUM ION × 8 ZN ZINC ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；protein solution (11.0 mg/mL H8 in unbuffered 3.0MM NAN3), 2.5mL of precipitant buffer (0.1M sodium acetate (PH 4.6), 20%(v/v) isopropanol, 0.2M CaCl2), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. Soaking experiment performed with mercury ions using the mother liquor without calcium ions.
Resolution 3.06 Å R-free 0.256
3ES3 Directing Noble Metal Ion Chemistry within a Designed Ferritin Protein. The Complex with Gold ions. Ferritin H8-H9x Mutant Deposited 2008-10-03 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Mutation：H13D, E64C, K86Q, C90R, C102A, H105Q, C130S, E140C, K143C, E147C AU GOLD ION × 96 CA CALCIUM ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；298 K；Protein solution (11.0 mG/mL H8 in unbuffered 3.0MM NaN3), 2.5mL of precipitant buffer (0.1 M sodium acetate (PH 4.6), 20%(V/V) isopropanol, 0.2M CaCl2), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K. Soaking crystals were performed using a mother liquor (no calcium ions) with the addition of 0.5 mM AuCl3 for one week.
Resolution 2.79 Å R-free 0.275
4DYX Crystal Structure of the Cu-adduct of Human H-Ferritin variant 4His-delta C-star Deposited 2012-02-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Mutation：K86Q, C90E, C102A, C130A CU COPPER (II) ION × 96 CA CALCIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50 mM Tris, 5 mM calcium chloride, 200 microM cupric chloride , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.85 Å R-free 0.197
4DYY Crystal Structure of the Cu-adduct of Human H-Ferritin variant MIC1 Deposited 2012-02-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Mutation：L56H, R63H, E67H, K86Q, C90E, C102A, C130A CU COPPER (II) ION × 72 CA CALCIUM ION × 48 EDO 1,2-ETHANEDIOL × 24 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50 mM Tris, 5 mM calcium chloride, 8% PEG 1900 MME, 700 micro M cupric chloride, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.90 Å R-free 0.241
4DYZ Crystal Structure of the apo form of Human H-Ferritin variant MIC1 Deposited 2012-02-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Mutation：L56H, R63H, E67H, K86Q, C90E, C102A, C130A CU COPPER (II) ION × 24 CA CALCIUM ION × 96 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50 mM Tris, 10 mM calcium chloride, 4% PEG 400, soaked in 20 mM EDTA, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.30 Å R-free 0.272
4DZ0 Crystal structure of the Cu-adduct of human H-Ferritin variant MIC1 labeled with a dansyl fluorophore Deposited 2012-02-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa） Fragment：UNP residues 6-177
Mutation：K53C, L56H, R63H, E67H, K86Q, C90E, C102A, C130A AEN 5-(1-SULFONAPHTHYL)-ACETYLAMINO-ETHYLAMINE × 24 CU COPPER (II) ION × 72 CA CALCIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；50 mM Tris, 5 mM calcium chloride, 50 mM sodium chloride, 10% PEG 3350, 350 M cupric chloride, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 2.50 Å R-free 0.300
4OYN Fifteen minutes iron loaded human H ferritin Deposited 2014-02-12 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 24 BCN BICINE × 24 FE FE (III) ION × 168 CL CHLORIDE ION × 312 MG MAGNESIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；277 K；1.6 M MgCl2 and 0.1 M bicine pH 9.0
Resolution 1.43 Å R-free 0.179
4Y08 ONE MINUTE IRON LOADED HUMAN H FERRITIN Deposited 2015-02-05 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded FE2 FE (II) ION × 120 CL CHLORIDE ION × 216 MG MAGNESIUM ION × 120 OXY OXYGEN MOLECULE × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；281 K；2.0 M magnesium chloride and 0.1 M BICINE at pH 9.0
Resolution 1.34 Å R-free 0.173
4YKH Thirty minutes iron loaded human H ferritin Deposited 2015-03-04 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded BCN BICINE × 24 FE2 FE (II) ION × 168 MG MAGNESIUM ION × 96 CL CHLORIDE ION × 288 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；281 K；2.0 M magnesium chloride, 0.1 M Bicine pH 9.0
Resolution 1.52 Å R-free 0.187
4ZJK FIVE MINUTES IRON LOADED HUMAN H FERRITIN Deposited 2015-04-29 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa） Fragment：UNP residues 2-183
Not recorded FE2 FE (II) ION × 120 MG MAGNESIUM ION × 120 CL CHLORIDE ION × 336 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；281 K；0.1 Bicine pH 9.0, 2.0 M Magnesium Chloride
Resolution 1.56 Å R-free 0.192
5CMQ Crystal Structure of Zn-bound Human H-Ferritin variant 122H-delta C-star Deposited 2015-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa） Fragment：Ferritin-like diiron domain containing residues 6-177
Mutation：K86Q, C90E, C102A, C130A, T122H ZN ZINC ION × 216 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；298 K；25 mM Tris, 10 mM calcium chloride, 10 mM zinc chloride, 2% PEG 3350
Resolution 1.94 Å R-free 0.180
5CMR Crystal Structure of Linker-Mediated Zn-bound Human H-Ferritin variant 122H-delta C-star Deposited 2015-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa） Fragment：Ferritin-like diiron domain containing residues 6-178
Mutation：K86A, C90E, C102A, C130A, T122H ZN ZINC ION × 48 NA SODIUM ION × 72 BYD N,N'-dihydroxybenzene-1,4-dicarboxamide × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；50 mM CHES, 150 mM sodium chloride, 0.3 mM zinc chloride, 1 mM H2BDH
Resolution 3.79 Å R-free 0.256
5GN8 Structure of a 48-mer protein nanocage fabricated from its 24-mer analogue by subunit interface redesign Deposited 2016-07-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 48 PDB declaration: 48-meric
Chain A 2–183（182 aa）
Chain B 2–153（152 aa）
Not recorded CA CALCIUM ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；300 K；0.1 M imidazol-HCl at pH 7.5, 10% reagent alcohol (15%) and 0.2 M MgCl2
Resolution 2.81 Å R-free 0.251
5GOU Structure of a 16-mer protein nanocage fabricated from its 24-mer analogue by subunit interface redesign Deposited 2016-07-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 16 PDB declaration: hexadecameric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；300 K；1% PEG 4K, 1% MPD, 0.1M NaAC
Resolution 2.91 Å R-free 0.275
5JKK Crystal structure of the negatively supercharged variant Ftn(neg) of human heavy chain ferritin Deposited 2016-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Not recorded FE FE (III) ION × 30 MG MAGNESIUM ION × 51 CL CHLORIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.52 M magnesium acetate, 100 mM Tris, pH 8.5, 8 mg/mL Ftn(neg)
Resolution 1.60 Å R-free 0.143
5JKL Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (Mg formate condition) Deposited 2016-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Not recorded FE FE (III) ION × 36 MG MAGNESIUM ION × 32 CL CHLORIDE ION × 12 GOL GLYCEROL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.19 M magnesium formate, 4 mg/mL Ftn(pos) and 4 mg/mL Ftn(neg)
Resolution 1.80 Å R-free 0.176
5JKL Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (Mg formate condition) Deposited 2016-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded FE FE (III) ION × 36 MG MAGNESIUM ION × 24 CL CHLORIDE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.19 M magnesium formate, 4 mg/mL Ftn(pos) and 4 mg/mL Ftn(neg)
Resolution 1.80 Å R-free 0.176
5JKM Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (Mg acetate condition) Deposited 2016-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 32 GOL GLYCEROL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.20 M magnesium acetate, 100 mM Tris, pH 8.5, 8 mg/mL Ftn(pos) and 8 mg/mL Ftn(neg)
Resolution 1.80 Å R-free 0.191
5JKM Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (Mg acetate condition) Deposited 2016-04-26 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 36 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.20 M magnesium acetate, 100 mM Tris, pH 8.5, 8 mg/mL Ftn(pos) and 8 mg/mL Ftn(neg)
Resolution 1.80 Å R-free 0.191
5N26 X-ray structure of human heavy chain ferritin in complex with cisplatin Deposited 2017-02-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded CPT Cisplatin × 72 73M bis(azanyl)-chloranyl-oxidanyl-platinum × 24 CL CHLORIDE ION × 144 MG MAGNESIUM ION × 120 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M Magnesium chloride, 0.1 M bicine pH 9.0
Resolution 2.05 Å R-free 0.206
5N27 X-ray structure of human heavy chain ferritin (apo form) Deposited 2017-02-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded CL CHLORIDE ION × 144 MG MAGNESIUM ION × 192 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2.0 M MgCl2, 0.1 M bicine pH 9.0
Resolution 1.74 Å R-free 0.191
5UP7 Crystal Structure of the Ni-bound Human Heavy-Chain Ferritin 122H-delta C-star variant Deposited 2017-02-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded NI NICKEL (II) ION × 120 CA CALCIUM ION × 48 CL CHLORIDE ION × 24 EDO 1,2-ETHANEDIOL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8；293 K；Reservoir: 500 uL total volume: 25 mM Tris (pH 8), 10 mM CaCl2, 1 mM NiCl2, 1% PEG 6000 Sitting Drop: 2 uL reservoir, 2 uL of 12.5 uM ferritin
Resolution 1.79 Å
5UP8 Crystal Structure of the Zn-bound Human Heavy-Chain variant 122H-delta C-star with para-benzenedihydroxamate Deposited 2017-02-01 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded ZN ZINC ION × 72 NA SODIUM ION × 24 BYD N,N'-dihydroxybenzene-1,4-dicarboxamide × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 8.5), 150 mM NaCl, 0.14 mM ZnCl2 Sitting Drop: 8.6 uL reservoir, 1 uL of 12.5 uM ferritin, 2.4 uL of 5 mM p-H2bdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.63 Å R-free 0.262
5UP9 Crystal Structure of Zn-bound Human Heavy-Chain ferritin variant 122H-delta C-star with para-xylenedihydroxamate Deposited 2017-02-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Not recorded ZN ZINC ION × 76 PGE TRIETHYLENE GLYCOL × 20 PEG DI(HYDROXYETHYL)ETHER × 76 BYX 2,2'-(1,4-phenylene)bis(N-hydroxyacetamide) × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 8.5), 150 mM NaCl, 0.474 mM ZnCl2, 3% PEG 300 Sitting Drop: 7.6 uL reservoir, 2 uL of 12.5 uM ferritin, 2.4 uL of 5 mM p-H2xdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.45 Å R-free 0.289
5VTD Crystal Structure of the Co-bound Human Heavy-Chain Ferritin variant 122H-delta C-star Deposited 2017-05-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded CO COBALT (II) ION × 120 CL CHLORIDE ION × 24 CA CALCIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；295 K；Reservoir: 500 uL total volume: 25 mM Tris (pH 8), 12 mM CaCl2, 150 mM NaCl, 0.3 mM CoCl2, 1% PEG 1900 MME Sitting Drop: 2 uL reservoir, 2 uL of 4 uM ferritin
Resolution 1.95 Å R-free 0.217
5XB1 human ferritin mutant - E-helix deletion Deposited 2017-03-15 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–160（160 aa） Fragment：UNP residues 6-160
Chain B 1–160（160 aa） Fragment：UNP residues 6-160
Chain C 1–160（160 aa） Fragment：UNP residues 6-160
Chain D 1–160（160 aa） Fragment：UNP residues 6-160
Chain E 1–160（160 aa） Fragment：UNP residues 6-160
Chain F 1–160（160 aa） Fragment：UNP residues 6-160
Chain G 1–160（160 aa） Fragment：UNP residues 6-160
Chain H 1–160（160 aa） Fragment：UNP residues 6-160
Chain I 1–160（160 aa） Fragment：UNP residues 6-160
Chain J 1–160（160 aa） Fragment：UNP residues 6-160
Chain K 1–160（160 aa） Fragment：UNP residues 6-160
Chain L 1–160（160 aa） Fragment：UNP residues 6-160
Chain M 1–160（160 aa） Fragment：UNP residues 6-160
Chain N 1–160（160 aa） Fragment：UNP residues 6-160
Chain O 1–160（160 aa） Fragment：UNP residues 6-160
Chain P 1–160（160 aa） Fragment：UNP residues 6-160
Chain Q 1–160（160 aa） Fragment：UNP residues 6-160
Chain R 1–160（160 aa） Fragment：UNP residues 6-160
Chain S 1–160（160 aa） Fragment：UNP residues 6-160
Chain T 1–160（160 aa） Fragment：UNP residues 6-160
Chain U 1–160（160 aa） Fragment：UNP residues 6-160
Chain V 1–160（160 aa） Fragment：UNP residues 6-160
Chain W 1–160（160 aa） Fragment：UNP residues 6-160
Chain X 1–160（160 aa） Fragment：UNP residues 6-160
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；buffers were titrated with HCl to pH8.0
cryo-EM vitrification conditions Cryogen ETHANE；blot for 9 seconds before plunging
Resolution 3.00 Å
5YI5 human ferritin mutant - E-helix deletion Deposited 2017-10-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–177（177 aa）
Chain B 1–177（177 aa）
Chain C 1–177（177 aa）
Chain D 1–177（177 aa）
Chain E 1–177（177 aa）
Chain F 1–177（177 aa）
Chain G 1–177（177 aa）
Chain H 1–177（177 aa）
Chain I 1–177（177 aa）
Chain J 1–177（177 aa）
Chain K 1–177（177 aa）
Chain L 1–177（177 aa）
Chain M 1–177（177 aa）
Chain N 1–177（177 aa）
Chain O 1–177（177 aa）
Chain P 1–177（177 aa）
Chain Q 1–177（177 aa）
Chain R 1–177（177 aa）
Chain S 1–177（177 aa）
Chain T 1–177（177 aa）
Chain U 1–177（177 aa）
Chain V 1–177（177 aa）
Chain W 1–177（177 aa）
Chain X 1–177（177 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2；buffers were titrated with HCl to pH7.2
cryo-EM vitrification conditions Cryogen ETHANE；blot for 9 seconds before plunging
Resolution 3.00 Å
5ZND 8-mer nanotube derived from 24-mer rHuHF nanocage Deposited 2018-04-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 1–134（134 aa）
Mutation：K86Q No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.2M ammonium citrate (pH=8.0), 0.1M Tris-HCl (pH=8.0), 22% (w/v) PEG 3350
Resolution 3.00 Å R-free 0.276
6B8F Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid Deposited 2017-10-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded FE FE (III) ION × 48 CA CALCIUM ION × 264 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Reservoir: 500 uL of 25 mM HEPES pH 7.0 with 10 mM CaCl2 Well: 2 uL of reservoir solution and 2 uL of 2.5 uM ferritin (by 24-mer) in 15 mM TRIS pH 7.4 with 150 mM NaCl After crystals formed, a crystal was harvested and soaked in a buffered solution comprised of 25 mM HEPES pH 7.0, 30 mM CaCl2, 8.6 % (w/v) sodium acrylate, 2.5 % (w/v) acrylamide, and 0.2 % (w/v) Bis-acrylamide overnight. Crystal was transferred to a solution containing 1 % APS and 1% TEMED with 4 M NaCl for 5 min. Crystal was then transferred to a clean slide and soaked in 30 uL H2O for 5 min. This solution was removed and the crystal was soaked in 1 M CaCl2 for 2 min. The crystal was removed, cryoprotected in perfluoro polyether, and frozen in liquid N2.
Resolution 1.06 Å R-free 0.103
6B8G Twice-Contracted Human Heavy-Chain Ferritin Crystal-Hydrogel Hybrid Deposited 2017-10-07 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded FE FE (III) ION × 48 CA CALCIUM ION × 264 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Reservoir: 500 uL of 25 mM HEPES pH 7.0 with 10 mM CaCl2 Well: 2 uL of reservoir solution and 2 uL of 2.5 uM ferritin (by 24-mer) in 15 mM TRIS pH 7.4 with 150 mM NaCl After crystals formed, a crystal was harvested and soaked in a buffered solution comprised of 25 mM HEPES pH 7.0, 30 mM CaCl2, 8.6 % (w/v) sodium acrylate, 2.5 % (w/v) acrylamide, and 0.2 % (w/v) Bis-acrylamide overnight. Crystal was transferred to a solution containing 1 % APS and 1% TEMED with 4 M NaCl for 5 min. Crystal was then transferred to a clean slide and soaked in 30 uL H2O for 5 min. The H2O was removed the crystal was soaked in 4 M NaCl for 2 min. The crystal was removed, and soaked in 30 uL H2O for 5 min. This solution was removed and the crystal was soaked in 1 M CaCl2 for 2 min. The crystal was removed, cryoprotected in perfluoro polyether, and frozen in liquid N2.
Resolution 1.13 Å R-free 0.121
6FTV X-ray structure of human heavy chain ferritin in complex with NAMI A Deposited 2018-02-23 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded CL CHLORIDE ION × 168 MG MAGNESIUM ION × 216 RU RUTHENIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；2.0 M MgCl2, 0.1 M bicine pH 9.0
Resolution 1.58 Å R-free 0.183
6GSR Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex at 5.5 Angstrom resolution. Deposited 2018-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain Aa 2–183（182 aa）
Chain Ac 2–183（182 aa）
Chain Ad 2–183（182 aa）
Chain Ae 2–183（182 aa）
Chain Af 2–183（182 aa）
Chain Ag 2–183（182 aa）
Chain Ah 2–183（182 aa）
Chain Ai 2–183（182 aa）
Chain Aj 2–183（182 aa）
Chain Ak 2–183（182 aa）
Chain Al 2–183（182 aa）
Chain Am 2–183（182 aa）
Chain An 2–183（182 aa）
Chain Ao 2–183（182 aa）
Chain Ap 2–183（182 aa）
Chain Ar 2–183（182 aa）
Chain As 2–183（182 aa）
Chain At 2–183（182 aa）
Chain Au 2–183（182 aa）
Chain Av 2–183（182 aa）
Chain Aw 2–183（182 aa）
Chain Ax 2–183（182 aa）
Chain Ay 2–183（182 aa）
Chain Az 2–183（182 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.50 Å
6H5I Single Particle Cryo-EM map of human Transferrin receptor 1 - H-Ferritin complex. Deposited 2018-07-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 26 PDB declaration: 26-meric
Chain Aa 6–177（172 aa）
Chain Ac 6–177（172 aa）
Chain Ad 6–177（172 aa）
Chain Ae 6–177（172 aa）
Chain Af 6–177（172 aa）
Chain Ag 6–177（172 aa）
Chain Ah 6–177（172 aa）
Chain Ai 6–177（172 aa）
Chain Aj 6–177（172 aa）
Chain Ak 6–177（172 aa）
Chain Al 6–177（172 aa）
Chain Am 6–177（172 aa）
Chain An 6–177（172 aa）
Chain Ao 6–177（172 aa）
Chain Ap 6–177（172 aa）
Chain Ar 6–177（172 aa）
Chain As 6–177（172 aa）
Chain At 6–177（172 aa）
Chain Au 6–177（172 aa）
Chain Av 6–177（172 aa）
Chain Aw 6–177（172 aa）
Chain Ax 6–177（172 aa）
Chain Ay 6–177（172 aa）
Chain Az 6–177（172 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.90 Å
6H6T Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (propandiol condition, coordination number 8) Deposited 2018-07-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Not recorded FE FE (III) ION × 24 ACT ACETATE ION × 4 MG MAGNESIUM ION × 8 ZN ZINC ION × 12 CL CHLORIDE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；100 mM sodium acetate pH 4.5, 42 % propanediol
Resolution 1.90 Å R-free 0.222
6H6T Binary crystal structure of positively and negatively supercharged variants Ftn(pos) and Ftn(neg) from human heavy chain ferritin (propandiol condition, coordination number 8) Deposited 2018-07-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded FE FE (III) ION × 24 ACT ACETATE ION × 4 ZN ZINC ION × 12 CL CHLORIDE ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.5；293 K；100 mM sodium acetate pH 4.5, 42 % propanediol
Resolution 1.90 Å R-free 0.222
6H6U Unitary crystal structure of the positively supercharged variant Ftn(pos) from human heavy chain ferritin (PEG 400 condition) Deposited 2018-07-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Not recorded FE FE (III) ION × 60 GOL GLYCEROL × 4 CA CALCIUM ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.22 M CaCl2, 0.1 M HEPES pH 7.5 M, 30% PEG 400
Resolution 2.00 Å R-free 0.308
6IPC Non-native human ferritin 8-mer Deposited 2018-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293.15 K；0.1 M HEPES pH 7.5; 10% PEG 6000; 5% MPD
Resolution 4.44 Å R-free 0.277
6IPC Non-native human ferritin 8-mer Deposited 2018-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion Mutation：C90A, C102A, C130A, 140~145 deletion MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293.15 K；0.1 M HEPES pH 7.5; 10% PEG 6000; 5% MPD
Resolution 4.44 Å R-free 0.277
6IPO Ferritin mutant C90A/C102A/C130A/D144C Deposited 2018-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 48 PDB declaration: 48-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Mutation：C90A/C102A/C130A/D144C Mutation：C90A/C102A/C130A/D144C MG MAGNESIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293.15 K；magnesium chloride, PEG 400, TRIS
Resolution 3.00 Å R-free 0.245
6IPP Non-native ferritin 8-mer mutant-C90A/C102A/C130A/D144C Deposited 2018-11-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 48 PDB declaration: 48-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Mutation：C90A/C102A/C130A/D144C Mutation：C90A/C102A/C130A/D144C FE FE (III) ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；293.17 K；Sodium chloride,MPD,TRIS
Resolution 2.70 Å R-free 0.232
6IPQ Non-native ferritin 8-mer mutant-C90A/C102A/C130A Deposited 2018-11-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：C90A/C102A/C130A MG MAGNESIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；200mM MgCl2, 3.4M 1,6-Hexanediol, 100mM Tris/HCl
Resolution 3.10 Å R-free 0.276
6J4A Human H chain ferritin with an extension peptide Deposited 2019-01-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；PEG 8000, Hepes, ethylene glycol
Resolution 3.99 Å R-free 0.351
6J7G Human H-ferritin mutant-C90A/C102A/C130A/D144C Deposited 2019-01-18 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Chain Q 2–183（182 aa）
Chain R 2–183（182 aa）
Chain S 2–183（182 aa）
Chain T 2–183（182 aa）
Chain W 2–183（182 aa）
Chain X 2–183（182 aa）
Chain Y 2–183（182 aa）
Chain Z 2–183（182 aa）
Chain a 2–183（182 aa）
Chain b 2–183（182 aa）
Chain e 2–183（182 aa）
Chain f 2–183（182 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；293 K；Amonium Sulfate, HEPES
Resolution 3.87 Å R-free 0.328
6JOB Ferritin variant with "GMG" motif Deposited 2019-03-20 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded No recorded non-water small molecule Experimental method not declared
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293.15 K；sodium citrate tribase dihydrate, 1,6-Hexanediol
Resolution 2.93 Å R-free 0.368
6KE2 ABloop reengineered Ferritin Nanocage Deposited 2019-07-03 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Mutation：Deletion,K84Q MG MAGNESIUM ION × 120 FE FE (III) ION × 48 CL CHLORIDE ION × 48 CA CALCIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；285 K；0.1M bincine pH 9.0, 2M MgCl2
Resolution 1.80 Å R-free 0.179
6KE4 ABloop reengineered Ferritin Nanocage Deposited 2019-07-03 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Mutation：Deletion,K84Q FE FE (III) ION × 48 MG MAGNESIUM ION × 72 CL CHLORIDE ION × 48 CA CALCIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；0.1M Bincine pH 9.0, 2M MgCl2
Resolution 2.30 Å R-free 0.236
6M52 Human apo ferritin frozen on TEM grid with amorphous carbon supporting film Deposited 2020-03-09 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Not recorded FE2 FE (II) ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.60 Å
6M54 Human apo ferritin frozen on TEM grid with Amorphous nickel titanium alloy supporting film Deposited 2020-03-09 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Not recorded FE2 FE (II) ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.40 Å
6WYF Crystal structure of Human H-chain Ferritin variant 157C Delta C-star Modified with a RAFT Agent Soaked in an Acrylate Solution Deposited 2020-05-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：K86Q, C90E, C102A, C130A, K157C RFT butyl 1-{[2-(2,5-dioxopyrrolidin-1-yl)ethyl]amino}-2-methyl-1-oxopropan-2-yl carbonotrithioate × 24 CA CALCIUM ION × 264 FE FE (III) ION × 48 NA SODIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；5 uL reservoir + 5 uL 25 uM 157C delta C-star Human H-chain Ferritin in 15 mM HEPES, pH 7.0 against reservoir of 500 uL 25 mM HEPES, pH 8.0, 10 mM calcium chloride, 140 mM sodium chloride
Resolution 1.25 Å R-free 0.131
6WYG Crystal structure of Human H-chain Ferritin variant 157C Delta C-star Modified with a RAFT agent Deposited 2020-05-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C FE FE (III) ION × 54 CA CALCIUM ION × 48 RFT butyl 1-{[2-(2,5-dioxopyrrolidin-1-yl)ethyl]amino}-2-methyl-1-oxopropan-2-yl carbonotrithioate × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；5 uL reservoir + 5 uL 25 uM 157C delta C-star Human H-chain Ferritin in 15 mM HEPES, pH 7.0 against reservoir of 500 uL 50 mM MES, pH 6.5, 6 mM calcium chloride
Resolution 2.27 Å R-free 0.260
6WYH Crystal structure of Human H-chain Ferritin variant 157C Delta C-star Modified with a RAFT Agent Soaked in an Acrylate Solution Deposited 2020-05-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C Mutation：K86Q, C90E, C102A, C130A, K157C FE FE (III) ION × 60 RFT butyl 1-{[2-(2,5-dioxopyrrolidin-1-yl)ethyl]amino}-2-methyl-1-oxopropan-2-yl carbonotrithioate × 24 CA CALCIUM ION × 42 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；5 uL reservoir + 5 uL of 25 uM 157C delta C-star Human H-chain Ferritin in 15 mM HEPES, pH 7.0 against reservoir of 500 uL 50 mM MES, pH 6.5, 6 mM calcium chloride; crystals soaked in 1 M sodium acrylate, 50 mM calcium chloride, 25 mM MES, pH 6.5
Resolution 2.22 Å R-free 0.245
6Z6U 1.25 A structure of human apoferritin obtained from Titan Mono-BCOR microscope Deposited 2020-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.25 Å
6Z9E 1.55 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope Deposited 2020-06-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.55 Å
6Z9F 1.56 A structure of human apoferritin obtained from data subset of Titan Mono-BCOR microscope Deposited 2020-06-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.56 Å
7A6A 1.15 A structure of human apoferritin obtained from Titan Mono- BCOR microscope Deposited 2020-08-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.15 Å
7A6B 1.33 A structure of human apoferritin obtained from Titan Mono- BCOR microscope Deposited 2020-08-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.33 Å
7CK8 Crystal structure of human ferritin heavy chain mutant C90S/C102S/C130S Deposited 2020-07-16 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S Mutation：C90S, C102S, C130S CL CHLORIDE ION × 90 MG MAGNESIUM ION × 58 GOL GLYCEROL × 12 OXY OXYGEN MOLECULE × 30 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；291 K；0.1 M Bicine, pH 9.0, 1.7-2.0 M MgCl2
Resolution 1.80 Å R-free 0.223
7CK9 Crystal structure of Doxorubicin loaded human ferritin heavy chain Deposited 2020-07-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Not recorded CL CHLORIDE ION × 96 MG MAGNESIUM ION × 72 OXY OXYGEN MOLECULE × 24 GOL GLYCEROL × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；0.1 M Bicine, pH 9.0, 1.7 - 2 M MgCl2
Resolution 1.60 Å R-free 0.169
7JGK Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 100K Deposited 2020-07-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded V9Y N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide × 24 NI NICKEL (II) ION × 72 NA SODIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 31 mM CHES (pH 10), 93 mM NaCl, 0.474 mM NiCl2, 12% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 10 mM H2fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.68 Å R-free 0.244
7JGL Crystal Structure of the Zn-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 100K Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Chain Q 2–183（182 aa）
Chain R 2–183（182 aa）
Chain S 2–183（182 aa）
Chain T 2–183（182 aa）
Chain U 2–183（182 aa）
Chain V 2–183（182 aa）
Chain W 2–183（182 aa）
Chain X 2–183（182 aa）
Not recorded ZN ZINC ION × 62 NA SODIUM ION × 8 V9Y N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 25 mM CHES (pH 8.5), 75 mM NaCl, 0.474 mM ZnCl2, 10% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 5 mM H2fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.34 Å R-free 0.278
7JGL Crystal Structure of the Zn-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 100K Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain a 2–183（182 aa）
Chain b 2–183（182 aa）
Chain c 2–183（182 aa）
Chain d 2–183（182 aa）
Chain e 2–183（182 aa）
Chain f 2–183（182 aa）
Chain g 2–183（182 aa）
Chain h 2–183（182 aa）
Chain i 2–183（182 aa）
Chain j 2–183（182 aa）
Chain k 2–183（182 aa）
Chain l 2–183（182 aa）
Chain m 2–183（182 aa）
Chain n 2–183（182 aa）
Chain o 2–183（182 aa）
Chain p 2–183（182 aa）
Chain q 2–183（182 aa）
Chain r 2–183（182 aa）
Chain s 2–183（182 aa）
Chain t 2–183（182 aa）
Chain u 2–183（182 aa）
Chain v 2–183（182 aa）
Chain w 2–183（182 aa）
Chain x 2–183（182 aa）
Not recorded ZN ZINC ION × 62 NA SODIUM ION × 8 V9Y N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 25 mM CHES (pH 8.5), 75 mM NaCl, 0.474 mM ZnCl2, 10% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 5 mM H2fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.34 Å R-free 0.278
7JGM Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with meta-benzenedihyrdoxamate Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Chain Q 2–183（182 aa）
Chain R 2–183（182 aa）
Chain S 2–183（182 aa）
Chain T 2–183（182 aa）
Chain U 2–183（182 aa）
Chain V 2–183（182 aa）
Chain W 2–183（182 aa）
Chain X 2–183（182 aa）
Not recorded NI NICKEL (II) ION × 38 NA SODIUM ION × 8 V9D N~1~,N~3~-dihydroxybenzene-1,3-dicarboxamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 40 mM CHES (pH 8.5), 120 mM NaCl, 0.474 mM NiCl2, 10% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 5 mM m-bdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.31 Å R-free 0.245
7JGM Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with meta-benzenedihyrdoxamate Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain a 2–183（182 aa）
Chain b 2–183（182 aa）
Chain c 2–183（182 aa）
Chain d 2–183（182 aa）
Chain e 2–183（182 aa）
Chain f 2–183（182 aa）
Chain g 2–183（182 aa）
Chain h 2–183（182 aa）
Chain i 2–183（182 aa）
Chain j 2–183（182 aa）
Chain k 2–183（182 aa）
Chain l 2–183（182 aa）
Chain m 2–183（182 aa）
Chain n 2–183（182 aa）
Chain o 2–183（182 aa）
Chain p 2–183（182 aa）
Chain q 2–183（182 aa）
Chain r 2–183（182 aa）
Chain s 2–183（182 aa）
Chain t 2–183（182 aa）
Chain u 2–183（182 aa）
Chain v 2–183（182 aa）
Chain w 2–183（182 aa）
Chain x 2–183（182 aa）
Not recorded NI NICKEL (II) ION × 38 NA SODIUM ION × 8 V9D N~1~,N~3~-dihydroxybenzene-1,3-dicarboxamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 40 mM CHES (pH 8.5), 120 mM NaCl, 0.474 mM NiCl2, 10% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 5 mM m-bdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.31 Å R-free 0.245
7JGN Crystal Structure of the Zn-bound Human Heavy-chain variant 122H-delta C-star with meta-benzenedihyrdoxamate collected at 100K Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Chain Q 2–183（182 aa）
Chain R 2–183（182 aa）
Chain S 2–183（182 aa）
Chain T 2–183（182 aa）
Chain U 2–183（182 aa）
Chain V 2–183（182 aa）
Chain W 2–183（182 aa）
Chain X 2–183（182 aa）
Not recorded ZN ZINC ION × 62 NA SODIUM ION × 8 V9D N~1~,N~3~-dihydroxybenzene-1,3-dicarboxamide × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 9.5), 150 mM NaCl, 0.474 mM ZnCl2, 12.6% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 10 mM m-bdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.07 Å R-free 0.229
7JGN Crystal Structure of the Zn-bound Human Heavy-chain variant 122H-delta C-star with meta-benzenedihyrdoxamate collected at 100K Deposited 2020-07-19 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain a 2–183（182 aa）
Chain b 2–183（182 aa）
Chain c 2–183（182 aa）
Chain d 2–183（182 aa）
Chain e 2–183（182 aa）
Chain f 2–183（182 aa）
Chain g 2–183（182 aa）
Chain h 2–183（182 aa）
Chain i 2–183（182 aa）
Chain j 2–183（182 aa）
Chain k 2–183（182 aa）
Chain l 2–183（182 aa）
Chain m 2–183（182 aa）
Chain n 2–183（182 aa）
Chain o 2–183（182 aa）
Chain p 2–183（182 aa）
Chain q 2–183（182 aa）
Chain r 2–183（182 aa）
Chain s 2–183（182 aa）
Chain t 2–183（182 aa）
Chain u 2–183（182 aa）
Chain v 2–183（182 aa）
Chain w 2–183（182 aa）
Chain x 2–183（182 aa）
Not recorded ZN ZINC ION × 62 NA SODIUM ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 9.5), 150 mM NaCl, 0.474 mM ZnCl2, 12.6% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 10 mM m-bdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 2.07 Å R-free 0.229
7JGO Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 278K Deposited 2020-07-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded V9Y N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide × 24 NI NICKEL (II) ION × 72 NA SODIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；298 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 9.5), 150 mM NaCl, 0.474 mM NiCl2, 12.6% PEP Sitting Drop: 12.7 uL reservoir, 3.3 uL of 25 uM ferritin, 4 uL of 10 mM fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 3.08 Å R-free 0.248
7JGP Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate at 318K Deposited 2020-07-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded NI NICKEL (II) ION × 72 NA SODIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9.5；293 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 9.5), 150 mM NaCl, 0.474 mM NiCl2, 12.6% PEP Sitting Drop: 7.6 uL reservoir, 2 uL of 25 uM ferritin, 2.4 uL of 5 mM H2fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 6.42 Å R-free 0.302
7JGQ Crystal Structure of the Ni-bound Human Heavy-chain variant 122H-delta C-star with 2,5-furandihyrdoxamate collected at 278K after one heating/cooling cycle Deposited 2020-07-19 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded V9Y N~2~,N~5~-dihydroxyfuran-2,5-dicarboxamide × 24 NI NICKEL (II) ION × 72 NA SODIUM ION × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 500 uL total volume: 50 mM CHES (pH 9.5), 150 mM NaCl, 0.474 mM NiCl2, 12.6% PEP Sitting Drop: 12.7 uL reservoir, 3.3 uL of 25 uM ferritin, 4 uL of 10 mM fdh in 50 mM CHES (pH 9.5) with 150 mM NaCl
Resolution 3.01 Å R-free 0.251
7K26 Crystal structure of Human H-chain Ferritin variant infused with Sodium Acrylate Deposited 2020-09-08 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Not recorded FE FE (III) ION × 24 NA SODIUM ION × 14 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；298 K；Reservoir: 525 uL total volume 100 uL of 500 mM HEPES pH 7.0, 125 uL of 1 M NH4OAc, 300 uL 2-Methyl-2,4-pentanediol Sitting drop: 5 uL reservoir, 5 uL of 25 uM dCs ferritin
Resolution 2.70 Å R-free 0.254
7K3V Apoferritin structure at 1.34 angstrom resolution determined from a 300 kV Titan Krios G3i electron microscope with K3 detector Deposited 2020-09-14 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded ZN ZINC ION × 254 NA SODIUM ION × 80 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；50 mM Tris-HCl (pH 8.0), 150 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.34 Å
7K3W Apoferritin structure at 1.36 angstrom resolution determined from a 300 kV Titan Krios G3i electron microscope with Falcon4 detector Deposited 2020-09-14 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded ZN ZINC ION × 270 NA SODIUM ION × 112 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；50 mM Tris-HCl (pH 8.0), 150 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.36 Å
7KE3 Heavy chain ferritin with C-terminal EBNA1 epitope Deposited 2020-10-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Not recorded TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12 FE FE (III) ION × 40 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289.15 K；0.1M HEPES pH 7.0, 30% Jeffamine M-600 pH 7.0
Resolution 2.20 Å R-free 0.271
7KE5 Heavy chain ferritin with N-terminal EBNA1 epitope Deposited 2020-10-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Not recorded TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 12 FE FE (III) ION × 32 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；289.15 K；0.1M ammonium citrate tribasic pH 7.0, 12% PEG 3350
Resolution 2.80 Å R-free 0.317
7PF1 UVC treated Human apoferritin Deposited 2021-08-11 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 4–177（174 aa）
Chain B 4–177（174 aa）
Chain C 4–177（174 aa）
Chain D 4–177（174 aa）
Chain E 4–177（174 aa）
Chain F 4–177（174 aa）
Chain G 4–177（174 aa）
Chain H 4–177（174 aa）
Chain I 4–177（174 aa）
Chain J 4–177（174 aa）
Chain K 4–177（174 aa）
Chain L 4–177（174 aa）
Chain M 4–177（174 aa）
Chain N 4–177（174 aa）
Chain O 4–177（174 aa）
Chain P 4–177（174 aa）
Chain Q 4–177（174 aa）
Chain R 4–177（174 aa）
Chain S 4–177（174 aa）
Chain T 4–177（174 aa）
Chain U 4–177（174 aa）
Chain V 4–177（174 aa）
Chain W 4–177（174 aa）
Chain X 4–177（174 aa）
Not recorded CL CHLORIDE ION × 96 MG MAGNESIUM ION × 167 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.10 Å
7R5O 1.58 A STRUCTURE OF HUMAN APOFERRITIN OBTAINED FROM TITAN KRIOS 2 AT eBIC, DLS UNDER COMMISSIONING SESSION CM26464-2 Deposited 2022-02-11 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain U 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；50 mM Tris-HCl, pH 7.5, 100 mM NaCl, 1 mM TCEP
cryo-EM vitrification conditions Cryogen ETHANE；blot time of 2.5 seconds
Resolution 1.60 Å
7RRP Apoferritin structure at 1.27 angstrom resolution determined from a 300 kV Titan Krios G3i electron microscope with Falcon4 detector Deposited 2021-08-10 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded ZN ZINC ION × 206 NA SODIUM ION × 72 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；50 mM Tris-HCl (pH 8.0), 150 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.27 Å
7V66 Structure of Apoferritin Deposited 2021-08-19 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.89 Å
7VD8 1.96 A structure of human apoferritin obtained from Talos Arctica microscope Deposited 2021-09-06 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded ZN ZINC ION × 254 NA SODIUM ION × 75 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.96 Å
7ZG7 Structure of human Apoferritin obtained from ssDNA coated grid Deposited 2022-04-02 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded ZN ZINC ION × 270 NA SODIUM ION × 112 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；6 s blot time,30 s waiting time, ssDNA covered grid
Resolution 1.77 Å
8A2L X-ray structure of TRIL-encapsulated human heavy chain ferritin Deposited 2022-06-03 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 5 MG MAGNESIUM ION × 6 FE FE (III) ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M magnesium chloride, 0.1 M bicine buffer pH 9.0
Resolution 2.30 Å R-free 0.224
8A2M X-ray structure of Ru(bpy)3]2+ complex (Ru1)-encapsulated human heavy chain ferritin Deposited 2022-06-03 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 192 MG MAGNESIUM ION × 192 FE FE (III) ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M magnesium chloride, 0.1 M bicine buffer pH 9.0
Resolution 1.57 Å R-free 0.190
8A5N X-ray structure of human H-chain ferritin treated with SDS Deposited 2022-06-15 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 240 GOL GLYCEROL × 24 FE FE (III) ION × 24 MG MAGNESIUM ION × 240 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M magnesium chloride 0.1 M bicine buffer pH 9.0
Resolution 1.52 Å R-free 0.190
8AAV Human heavy chain ferritin with introduced Cys residues modified with C10 ligand Deposited 2022-07-03 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Not recorded O3K 2-bromanyl-N-decyl-ethanamide × 48 FE FE (III) ION × 24 MG MAGNESIUM ION × 45 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；Crystallization of little amounts of protein or functionalized protein variants were performed via hanging drop vapor diffusion techniques. Reservoir solution (100 mM Tris, 500 mM MgOAc, pH 8.5) was prepared in a 24- well manual plate set. Drops were prepared on siliconized glass cover slides (Jena Bioscience) by mixing 2 microL reservoir solutions with 1 microL 50 mM Tris, 1 M NaCl, pH 7.5 buffer and 1 microL of respective ferritin variant. Plates were incubated at 298K. After one day first crystals were visible.
Resolution 2.00 Å R-free 0.177
8B7O X-ray structure of Auranofin-human H-chain ferritin Deposited 2022-09-30 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 144 MG MAGNESIUM ION × 192 FE FE (III) ION × 24 AU GOLD ION × 120 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M magnesium chloride 0.1 M Bicine buffer pH 9.0
Resolution 1.17 Å R-free 0.167
8CPM Human apoferritin after 405 nm laser exposure Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.81 Å
8CPS Human apoferritin Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.82 Å
8CPT Human apoferritin after 488 nm laser exposure Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.79 Å
8CPU Human apoferritin after 561 nm laser exposure Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.76 Å
8CPV Human apoferritin Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.76 Å
8CPW Human apoferritin after 405 nm + 488 nm laser exposure in presence of rsEGFP2 Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.79 Å
8CPX Human apoferritin after 488 nm laser exposure in presence of rsEGFP2 Deposited 2023-03-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 5–177（173 aa）
Chain 2 5–177（173 aa）
Chain 4 5–177（173 aa）
Chain 6 5–177（173 aa）
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain K 5–177（173 aa）
Chain M 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain S 5–177（173 aa）
Chain U 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Chain a 5–177（173 aa）
Chain e 5–177（173 aa）
Chain r 5–177（173 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 MG MAGNESIUM ION × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.76 Å
8DHX Human liver ferritin Deposited 2022-06-28 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain 1 1–183（183 aa）
Chain 2 1–183（183 aa）
Chain 4 1–183（183 aa）
Chain 6 1–183（183 aa）
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain K 1–183（183 aa）
Chain M 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain S 1–183（183 aa）
Chain U 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Chain Y 1–183（183 aa）
Chain a 1–183（183 aa）
Chain e 1–183（183 aa）
Chain r 1–183（183 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.92 Å
8DNP Human Brain Ferritin Heavy Chain Deposited 2022-07-11 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Not recorded FE FE (III) ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.69 Å
8F49 1.8 angstrom structure of apoferritin embedded in crystalline ice Deposited 2022-11-10 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
Resolution 1.80 Å
8F4L Structure of human apoferritin embedded in crystalline ice Deposited 2022-11-11 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE；Apo-ferritin embedded in crystalline ice.
Resolution 2.40 Å
8HHS Structure of human apoferritin embedded in crystalline ice Deposited 2022-11-17 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Chain M 6–177（172 aa）
Chain N 6–177（172 aa）
Chain O 6–177（172 aa）
Chain P 6–177（172 aa）
Chain Q 6–177（172 aa）
Chain R 6–177（172 aa）
Chain S 6–177（172 aa）
Chain T 6–177（172 aa）
Chain U 6–177（172 aa）
Chain V 6–177（172 aa）
Chain W 6–177（172 aa）
Chain X 6–177（172 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
Resolution 2.40 Å
8J9L Crystal Structure of Human H-Ferritin variant 123F assembling in solution2 Deposited 2023-05-04 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F FE FE (III) ION × 32 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 9.5；293 K；50 mM BICINE pH 9.5, 800 mM sodium chloride
Resolution 2.50 Å R-free 0.289
8J9M Crystal Structure of Human H-Ferritin variant 123F assembling in solution3 Deposited 2023-05-04 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Mutation：D123F Mutation：D123F Mutation：D123F FE FE (III) ION × 64 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；50 mM TRIS-HCL pH 7.5, 200 mM Sodium chloride
Resolution 2.90 Å R-free 0.243
8JAI Crystal Structure of Human H-Ferritin variant 123F assembling in solution 1 Deposited 2023-05-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F Mutation：D123F FE FE (III) ION × 18 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 9.5；293 K；50 mM CAPS pH 9.5, 200 mM Sodium chloride
Resolution 2.56 Å R-free 0.368
8KFD Ferritin drug carrier(FDC) for encapsulated platinum (IV) prodrug for esophageal squamous cell carcinoma targeted therapy Deposited 2023-08-15 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded PT PLATINUM (II) ION × 24 GOL GLYCEROL × 72 CA CALCIUM ION × 24 CL CHLORIDE ION × 288 MG MAGNESIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；291 K；1.6-1.9 M MgCl2 and 0.1 M Bicine pH 9.0
Resolution 1.80 Å R-free 0.166
8PP2 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and native(K86Q) human heavy chain ferritin (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R Mutation：K86Q, A18K, C90K, N98R, C102K, H105K, N25R, N109K, D123K, E162R GOL GLYCEROL × 20 FE FE (III) ION × 24 MG MAGNESIUM ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium Formate Ftn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaCl Ftn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl 2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(Wildtype) added to coverslide in this order.
Resolution 2.00 Å R-free 0.247
8PP2 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and native(K86Q) human heavy chain ferritin (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 6–177（172 aa）
Chain H 6–177（172 aa）
Chain I 6–177（172 aa）
Chain J 6–177（172 aa）
Chain K 6–177（172 aa）
Chain L 6–177（172 aa）
Mutation：K86Q Mutation：K86Q Mutation：K86Q Mutation：K86Q Mutation：K86Q Mutation：K86Q FE FE (III) ION × 24 MG MAGNESIUM ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium Formate Ftn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaCl Ftn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl 2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(Wildtype) added to coverslide in this order.
Resolution 2.00 Å R-free 0.247
8PP3 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and crystal contact tuned negatively supercharged ferritin variant Ftn(neg)-m1 (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R FE FE (III) ION × 24 GOL GLYCEROL × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium FormateFtn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaClFtn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(Wildtype) added to coverslide in this order.
Resolution 1.55 Å R-free 0.241
8PP3 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and crystal contact tuned negatively supercharged ferritin variant Ftn(neg)-m1 (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Mutation：C90E, C102E, H105E Mutation：C90E, C102E, H105E Mutation：C90E, C102E, H105E Mutation：C90E, C102E, H105E Mutation：C90E, C102E, H105E Mutation：C90E, C102E, H105E FE FE (III) ION × 24 MG MAGNESIUM ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium FormateFtn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaClFtn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(Wildtype) added to coverslide in this order.
Resolution 1.55 Å R-free 0.241
8PP4 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and reduced charge negatively supercharged ferritin variant Ftn(neg)-m3 (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：A18K, C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R FE FE (III) ION × 28 MG MAGNESIUM ION × 12 CL CHLORIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium FormateFtn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaClFtn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(neg)-m3 added to coverslide in this order.
Resolution 2.00 Å R-free 0.221
8PP4 Binary crystal structure of positively supercharged ferritin variant Ftn(pos) and reduced charge negatively supercharged ferritin variant Ftn(neg)-m3 (Mg formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Mutation：A18E Mutation：A18E Mutation：A18E Mutation：A18E Mutation：A18E Mutation：A18E FE FE (III) ION × 28 MG MAGNESIUM ION × 16 CL CHLORIDE ION × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium FormateFtn(pos): 4 mg/mL in 50mM Tris pH 7.5 1 M NaClFtn(Wildtype): 4mg/mL in 50mM Tris pH 7.5 0.3 M NaCl2 uL reservoir + 1uL Ftn(pos) + 1uL Ftn(neg)-m3 added to coverslide in this order.
Resolution 2.00 Å R-free 0.221
8PP5 Unitary crystal structure of positively supercharged ferritin variant Ftn(pos)-m1 (Mg Formate condition) Deposited 2023-07-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Chain B 6–177（172 aa）
Chain C 6–177（172 aa）
Chain D 6–177（172 aa）
Chain E 6–177（172 aa）
Chain F 6–177（172 aa）
Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R Mutation：C90K, N98R, C102K, H105K N25R, N109K, D123K, E162R FE FE (III) ION × 24 MG MAGNESIUM ION × 16 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293.15 K；reservoir: 0.19M Magnesium Formate Ftn(pos)-m1: 4 mg/mL in 50mM Tris pH 7.5 0.9 M NaCl 2microliter reservoir + 1microliter Ftn(pos)-m1 +1 microliterL 50mM Tris pH 7.5 0.3 M NaCl
Resolution 2.00 Å R-free 0.193
8QU9 Structure of the NCOA4 (Nuclear Receptor Coactivator 4)-FTH1 (H-Ferritin) complex Deposited 2023-10-15 Different construct Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric
Chain A 6–183（178 aa）
Not recorded FE FE (III) ION × 48 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.88 Å
8W92 human H ferritin with 2 Fe(II)/subunit loading Deposited 2023-09-04 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded FE FE (III) ION × 72 CA CALCIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM HEPES, pH7, 20 mM CaCl2
Resolution 2.12 Å R-free 0.200
8WB3 Human H Chain Ferritin mutant-K86Q with 2 Fe(III)/subunit loading Deposited 2023-09-08 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Mutation：K86Q FE FE (III) ION × 48 CA CALCIUM ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；100 mM HEPES, pH7, 20 mM CaCl2
Resolution 2.49 Å R-free 0.235
8WIE Peptide 10-1/FTH1-1 Complex Deposited 2023-09-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–177（177 aa）
Chain B 1–177（177 aa）
Chain C 1–177（177 aa）
Chain D 1–177（177 aa）
Chain E 1–177（177 aa）
Chain F 1–177（177 aa）
Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N Mutation：Q15R,R23K,N26T,K87Q,N110E,S114E,E117N FE FE (III) ION × 4 CA CALCIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；289 K；1.5M Sodium chloride , 15% Ethanol and 20% PEG 3350
Resolution 2.30 Å R-free 0.212
8WIQ NCOA4/FTH1 complex Deposited 2023-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；250mM NaCl, 50mM Tris-HCL, pH 8.0
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.19 Å
8WJF Peptide 10/FTH1 complex Deposited 2023-09-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q Mutation：K87Q No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；250mM NaCl, 50mM Tris-HCL, pH 8.0
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.02 Å
8XWB Crystal structure of dinitrosyl iron units binding with human heavy chain Ferritin Deposited 2024-01-16 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Not recorded FE FE (III) ION × 96 MG MAGNESIUM ION × 72 CL CHLORIDE ION × 72 NO NITRIC OXIDE × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；Bicine,Magnesium chloride
Resolution 1.69 Å R-free 0.195
9EQC Iron loaded human h-chain ferritin exposed to oxygen for 20 minutes Deposited 2024-03-21 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded FE FE (III) ION × 144 MG MAGNESIUM ION × 144 CL CHLORIDE ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；0.1 M bicine 2.0 M magnesium chloride 100 mM sodiem chloride 60 mM ferrous chloride 3 mM sodium azide pH 9.0
Resolution 1.60 Å R-free 0.237
9HQ6 Structural insights in the HuHf@gold-monocarbene adduct: aurophilicity revealed in a biological context Deposited 2024-12-16 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Chain B 2–183（182 aa）
Chain C 2–183（182 aa）
Chain D 2–183（182 aa）
Chain E 2–183（182 aa）
Chain F 2–183（182 aa）
Chain G 2–183（182 aa）
Chain H 2–183（182 aa）
Chain I 2–183（182 aa）
Chain J 2–183（182 aa）
Chain K 2–183（182 aa）
Chain L 2–183（182 aa）
Chain M 2–183（182 aa）
Chain N 2–183（182 aa）
Chain O 2–183（182 aa）
Chain P 2–183（182 aa）
Chain Q 2–183（182 aa）
Chain R 2–183（182 aa）
Chain S 2–183（182 aa）
Chain T 2–183（182 aa）
Chain V 2–183（182 aa）
Chain W 2–183（182 aa）
Chain X 2–183（182 aa）
Chain Y 2–183（182 aa）
Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE Mutation：NONE BM0 1-butyl-3-methyl-1H-imidazol-3-ium × 24 AU GOLD ION × 96 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.51 Å
9I1B Iron loaded human H-chain ferritin 20 minute oxygen soak Deposited 2025-01-16 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 47 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded FE FE (III) ION × 141 CL CHLORIDE ION × 47 MG MAGNESIUM ION × 282 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；0.1 M Bicine 2 M Magnesium chloride 0.1 M Sodium chloride 60 mM Ferrous chloride 3 mM Sodium azide
Resolution 1.63 Å R-free 0.214
9I1C Iron loaded human H-chain ferritin 5 minute oxygen soak Deposited 2025-01-16 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: monomeric
Chain A 1–183（183 aa）
Not recorded FE FE (III) ION × 96 MG MAGNESIUM ION × 240 CL CHLORIDE ION × 72 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；0.1 M Bicine 2 M Magnesium chloride 100 mM Sodium chloride 60 mM Ferrous chloride 3 mM Sodium azide
Resolution 1.58 Å R-free 0.186
9I1E Iron loaded human H-chain ferritin D131N mutant 20 minute oxygen soak Deposited 2025-01-16 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded FE FE (III) ION × 72 CL CHLORIDE ION × 48 MG MAGNESIUM ION × 120 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；289 K；0.1 M Bicine 2 M Magnesium chloride 0.1 M Sodium chloride 60 mM Ferrous chloride 3 mM Sodium chloride
Resolution 1.76 Å R-free 0.190
9IVP 24-mer DARPin-apoferritin scaffold in complex with the maltose binding protein Deposited 2024-07-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric
Chain A 20–177（158 aa）
Chain BA 20–177（158 aa）
Chain C 20–177（158 aa）
Chain DA 20–177（158 aa）
Chain E 20–177（158 aa）
Chain FA 20–177（158 aa）
Chain G 20–177（158 aa）
Chain HA 20–177（158 aa）
Chain I 20–177（158 aa）
Chain JA 20–177（158 aa）
Chain K 20–177（158 aa）
Chain LA 20–177（158 aa）
Chain M 20–177（158 aa）
Chain NA 20–177（158 aa）
Chain O 20–177（158 aa）
Chain PA 20–177（158 aa）
Chain Q 20–177（158 aa）
Chain RA 20–177（158 aa）
Chain S 20–177（158 aa）
Chain TA 20–177（158 aa）
Chain V 20–177（158 aa）
Chain VA 20–177（158 aa）
Chain X 20–177（158 aa）
Chain Z 20–177（158 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9J48 GFP bound to 24-mer DARPin-apoferritin model 6c Deposited 2024-08-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 48 PDB declaration: 48-meric
Chain A 16–177（162 aa）
Chain B 16–177（162 aa）
Chain C 16–177（162 aa）
Chain D 16–177（162 aa）
Chain E 16–177（162 aa）
Chain F 16–177（162 aa）
Chain G 16–177（162 aa）
Chain H 16–177（162 aa）
Chain I 16–177（162 aa）
Chain J 16–177（162 aa）
Chain K 16–177（162 aa）
Chain L 16–177（162 aa）
Chain M 16–177（162 aa）
Chain N 16–177（162 aa）
Chain O 16–177（162 aa）
Chain P 16–177（162 aa）
Chain Q 16–177（162 aa）
Chain R 16–177（162 aa）
Chain S 16–177（162 aa）
Chain T 16–177（162 aa）
Chain V 16–177（162 aa）
Chain W 16–177（162 aa）
Chain X 16–177（162 aa）
Chain Y 16–177（162 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.04 Å
9JGO Structure of Pd ions bound to human heavy chain ferritin nanocage. Deposited 2024-09-08 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded MG MAGNESIUM ION × 72 PD PALLADIUM ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；283 K；2 M MgCl2, 0.1 M Bicine, pH 9.0
Resolution 1.85 Å R-free 0.197
9JGP Structure of Pd ions bound to human heavy chain ferritin nanocage. Deposited 2024-09-08 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Not recorded NA SODIUM ION × 96 MG MAGNESIUM ION × 96 PD PALLADIUM ION × 48 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；283 K；2 M MgCl2, 0.1 M Bicine, pH 9.0
Resolution 1.53 Å R-free 0.184
9JIU Ferritin mutant R63MeHis Deposited 2024-09-12 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 12-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63H Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 36 P6G HEXAETHYLENE GLYCOL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；293 K；0.1M Bicine pH 8.5, 20%(v/v) PEG 300
Resolution 2.28 Å R-free 0.272
9JQB Cryo-EM structure of ferritin variant R63BrThA/E67BrThA Deposited 2024-09-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.78 Å
9JQC Cryo-EM structure of ferritin variant R63BrThA/E67BrThA with Cu(II) Deposited 2024-09-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63BrThA/E67BrThA Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.73 Å
9JQD Cryo-EM structure of ferritin variant R63MeH/R67MeH Deposited 2024-09-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) FE FE (III) ION × 48 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.81 Å
9JQE Cryo-EM structure of ferritin variant R63MeH/R67MeH with Cu(II) Deposited 2024-09-27 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Chain I 1–183（183 aa）
Chain J 1–183（183 aa）
Chain K 1–183（183 aa）
Chain L 1–183（183 aa）
Chain M 1–183（183 aa）
Chain N 1–183（183 aa）
Chain O 1–183（183 aa）
Chain P 1–183（183 aa）
Chain Q 1–183（183 aa）
Chain R 1–183（183 aa）
Chain S 1–183（183 aa）
Chain T 1–183（183 aa）
Chain U 1–183（183 aa）
Chain V 1–183（183 aa）
Chain W 1–183（183 aa）
Chain X 1–183（183 aa）
Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R63MeH/R67MeH Non-standard monomer：Yes (specific site not provided by mmCIF) CU COPPER (II) ION × 48 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.83 Å
9KAY Bioengineered protein nanocarrier facilitating siRNA escape from lysosomes for targeted RNAi therapy in glioblastoma Deposited 2024-10-30 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain Aa 2–160（159 aa）
Chain Ab 2–160（159 aa）
Chain Ac 2–160（159 aa）
Chain Ad 2–160（159 aa）
Chain Ae 2–160（159 aa）
Chain Af 2–160（159 aa）
Chain Ag 2–160（159 aa）
Chain Ah 2–160（159 aa）
Chain Ai 2–160（159 aa）
Chain Aj 2–160（159 aa）
Chain Ak 2–160（159 aa）
Chain Al 2–160（159 aa）
Chain Am 2–160（159 aa）
Chain An 2–160（159 aa）
Chain Ao 2–160（159 aa）
Chain Ap 2–160（159 aa）
Chain Aq 2–160（159 aa）
Chain Ar 2–160（159 aa）
Chain As 2–160（159 aa）
Chain At 2–160（159 aa）
Chain Au 2–160（159 aa）
Chain Av 2–160（159 aa）
Chain Aw 2–160（159 aa）
Chain Ax 2–160（159 aa）
Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K Mutation：E61K,E64R,E140K,E147K No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8；20 mM Tris, pH8.0, 50 mM NaCl
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.73 Å
9LNY Crystal structure of human heavy chain Ferritin binding with dinitrosyl iron complex modificated by phenylboronic acid Deposited 2025-01-22 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Not recorded FE FE (III) ION × 96 MG MAGNESIUM ION × 72 CL CHLORIDE ION × 72 NO NITRIC OXIDE × 48 A1EKS [3-(bromomethyl)phenyl]boronic acid × 24 H2S HYDROSULFURIC ACID × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；Bicine,Magnesium chloride
Resolution 2.40 Å R-free 0.242
9LNY Crystal structure of human heavy chain Ferritin binding with dinitrosyl iron complex modificated by phenylboronic acid Deposited 2025-01-22 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 6–177（172 aa）
Not recorded FE FE (III) ION × 96 MG MAGNESIUM ION × 72 CL CHLORIDE ION × 72 NO NITRIC OXIDE × 48 A1EKS [3-(bromomethyl)phenyl]boronic acid × 24 H2S HYDROSULFURIC ACID × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；Bicine,Magnesium chloride
Resolution 2.40 Å R-free 0.242
9LUW Enhancing Monodispersity and Thermal Stability of Human H-Ferritin for Improved Applications in Nanocarrier Systems Deposited 2025-02-10 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Chain B 1–183（183 aa）
Chain C 1–183（183 aa）
Chain D 1–183（183 aa）
Chain E 1–183（183 aa）
Chain F 1–183（183 aa）
Chain G 1–183（183 aa）
Chain H 1–183（183 aa）
Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H Mutation：C90A, C102A, H105A, E116A, T122H, C130A, L165H FE FE (III) ION × 42 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；sodium phosphate monobasic , potassium phosphate dibasic, imidazole, NaCl
Resolution 2.00 Å R-free 0.209
9RGH X-ray structure of a polyoxidovanadate/human H-ferritin adduct obtained when the protein is treated overnight with [VIVO(acac)2] Deposited 2025-06-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 144 MG MAGNESIUM ION × 144 A1JGJ Polyoxidovanadate complex × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M magnesium chloride, 0.1 M bicine buffer pH 9.0
Resolution 1.38 Å R-free 0.177
9RGI X-ray structure of a polyoxidovanadate/human H-ferritin adduct obtained when the protein is treated 6 days with [VIVO(acac)2] Deposited 2025-06-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 144 MG MAGNESIUM ION × 144 A1JGJ Polyoxidovanadate complex × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M bicine buffer pH 9.0, 2.0 M magnesium chloride
Resolution 1.54 Å R-free 0.198
9RGJ X-ray structure of a polyoxidovanadate/human H-ferritin adduct obtained when the protein is treated 24 h with [VIVO(acac)2] Deposited 2025-06-06 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain AAA 2–183（182 aa）
Not recorded CL CHLORIDE ION × 168 MG MAGNESIUM ION × 144 A1JGJ Polyoxidovanadate complex × 24 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；2.0 M MAGNESIUM CHLORIDE, 0.1 M bicine buffer pH 9.0
Resolution 1.50 Å R-free 0.196
9SJR Cryo-EM structure of Human Apoferritin at pH 3.5 Deposited 2025-09-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 3.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.99 Å
9SJS Cryo-EM structure of Human Apoferritin at pH 4 Deposited 2025-09-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.06 Å
9SJT Cryo-EM structure of Human Apoferritin at pH 5 Deposited 2025-09-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.96 Å
9SJU Cryo-EM structure of Human Apoferritin at pH 7 Deposited 2025-09-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.08 Å
9SJV Cryo-EM structure of Human Apoferritin at pH 9 Deposited 2025-09-01 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 5–177（173 aa）
Chain B 5–177（173 aa）
Chain C 5–177（173 aa）
Chain D 5–177（173 aa）
Chain E 5–177（173 aa）
Chain F 5–177（173 aa）
Chain G 5–177（173 aa）
Chain H 5–177（173 aa）
Chain I 5–177（173 aa）
Chain J 5–177（173 aa）
Chain K 5–177（173 aa）
Chain L 5–177（173 aa）
Chain M 5–177（173 aa）
Chain N 5–177（173 aa）
Chain O 5–177（173 aa）
Chain P 5–177（173 aa）
Chain Q 5–177（173 aa）
Chain R 5–177（173 aa）
Chain S 5–177（173 aa）
Chain T 5–177（173 aa）
Chain V 5–177（173 aa）
Chain W 5–177（173 aa）
Chain X 5–177（173 aa）
Chain Y 5–177（173 aa）
Not recorded FE FE (III) ION × 24 MG MAGNESIUM ION × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 9
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 1.89 Å
9VO7 Crystal structure of HuHF-C1, a HuHF varitant Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/E63A/H66A/K87Q/E108A/Y138A/Q142A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å R-free 0.257
9VOC Crystal strucrue of HuHF-C2, a variant of HuHF Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/Y55A/H58A/Q59A/E62A/E63A/H66A/K69A/K87Q/E108A/H137A/Y138A/E141A/Q142A/K144A/E148A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.224
9VOD Crystal strucrue of HuHF-C2-Cur complex 1 Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/Y55A/H58A/Q59A/E62A/E63A/H66A/K69A/K87Q/E108A/H137A/Y138A/E141A/Q142A/K144A/E148A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.92 Å R-free 0.192
9VOE Crystal strucrue of HuHF-C2-Cur complex 2 Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/Y55A/H58A/Q59A/E62A/E63A/H66A/K69A/K87Q/E108A/H137A/Y138A/E141A/Q142A/K144A/E148A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.220
9VOF Crystal strucrue of HuHF-C2-ALY complex Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/Y55A/H58A/Q59A/E62A/E63A/H66A/K69A/K87Q/E108A/H137A/Y138A/E141A/Q142A/K144A/E148A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å R-free 0.194
9VOM Crystal strucrue of HuHF-C2-AZB complex Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–183（182 aa）
Mutation：E28A/Y35A/Y55A/H58A/Q59A/E62A/E63A/H66A/K69A/K87Q/E108A/H137A/Y138A/E141A/Q142A/K144A/E148A No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.00 Å R-free 0.199
9VON Crystal strucrue of HuHF-71-Cur complex Deposited 2025-07-01 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 2–177（176 aa）
Chain B 2–177（176 aa）
Chain C 2–177（176 aa）
Chain D 2–177（176 aa）
Chain E 2–177（176 aa）
Chain F 2–177（176 aa）
Chain G 2–177（176 aa）
Chain H 2–177（176 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.50 Å R-free 0.237
9W28 Structure of Au3+ bound to human heavy chain ferritin nanocage. Deposited 2025-07-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.52 Å R-free 0.215
9W29 Structure of Au bound to human heavy chain ferritin nanocage. Deposited 2025-07-27 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 24 PDB declaration: 24-meric
Chain A 1–183（183 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.99 Å R-free 0.246

161 other PDB entries and 174 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FRIH_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–183； UniProt 1–183

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9i19

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9i19
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9i19
Deposition date deposition_date2025-01-16
最后修订 last_revision2026-01-28
Structure title titleIron loaded human H-chain ferritin D131N mutant 5 minute oxygen soak
Keywords keywordsIron, ferritin, H-chain, human, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.27 Å
Radius of gyration Rg (electron density) rg_electron18.45 Å
Forward intensity I(0) i08728320.00
Molecular weight molecular_weight20626.0 kDa
Excluded volume excluded_volume25291 ų
Envelope volume envelope_volume29908 ų
Hydration-shell volume shell_volume14549 ų
Envelope diameter envelope_diameter68.3 Å
Shell Rg shell_rg23.36 Å
Envelope Rg envelope_rg18.94 Å
Shape Rg shape_rg18.39 Å
Total Rg total_rg19.39 Å
Total atoms total_atoms1435
Residues n_residues174
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax72.5 Å
Rg (real space) rg_real19.42 Å
Rg uncertainty (real space) rg_real_error0.73 Å
I(0) (real space) i0_real8.7280e+06
I(0) uncertainty (real space) i0_real_error1.1390e+05
Rg (reciprocal space) rg_reciprocal19.40 Å
I(0) (reciprocal space) i0_reciprocal8728000.0000
Solution quality estimate total_estimate0.7753
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.1 Å
Skewness Skewness skewness0.548
Kurtosis Kurtosis kurtosis-0.198
Angular range angular_range— – 0.4150 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2398000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.504; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.564; Smooth: 1.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

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8. Citations (1)

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9. Files and Curves (10)