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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P16157 New Search
21PDB entries
31Biological assembly
32chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1N11 D34 REGION OF HUMAN ANKYRIN-R AND LINKER Deposited 2002-10-16 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 402–827（426 aa） Fragment：D34 region
Not recorded BR BROMIDE ION × 1 CL CHLORIDE ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；PEG400, HEPES, NaBr, CaCl2, acetonitrile, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.70 Å R-free 0.303
2YQF Solution structure of the death domain of Ankyrin-1 Deposited 2007-03-30 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1394–1497（104 aa） Fragment：death domain, UNP residues 1394-1497
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 120mM；Pressure ambient
NMR sample composition 20mM d-Tris-HCl(pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided
2YVI Crystal structure of a death domain of human ankryn protein Deposited 2007-04-12 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1394–1497（104 aa） Fragment：UNP residues 1394-1497, death domain
Not recorded GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.2M NaCl, 0.1M TrisCl pH8.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.92 Å R-free 0.217
2YVI Crystal structure of a death domain of human ankryn protein Deposited 2007-04-12 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1394–1497（104 aa） Fragment：UNP residues 1394-1497, death domain
Not recorded GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；298 K；0.2M NaCl, 0.1M TrisCl pH8.5, 25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K
Resolution 1.92 Å R-free 0.217
3F59 Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin Deposited 2008-11-03 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 911–1068（158 aa） Fragment：ZU5-ANK, spectrin binding region of human erythroid ankyrin: UNP residues 911-1068
Not recorded BR BROMIDE ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；20% PEG 4000, 0.25 M KBr, 10 mM DTT, 0.1 M MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.00 Å R-free 0.264
3F59 Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin Deposited 2008-11-03 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 911–1068（158 aa） Fragment：ZU5-ANK, spectrin binding region of human erythroid ankyrin: UNP residues 911-1068
Not recorded BR BROMIDE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；20% PEG 4000, 0.25 M KBr, 10 mM DTT, 0.1 M MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.00 Å R-free 0.264
3F59 Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin Deposited 2008-11-03 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 911–1068（158 aa） Fragment：ZU5-ANK, spectrin binding region of human erythroid ankyrin: UNP residues 911-1068
Not recorded BR BROMIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；20% PEG 4000, 0.25 M KBr, 10 mM DTT, 0.1 M MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.00 Å R-free 0.264
3F59 Crystal structure of ZU5-ANK, the spectrin binding region of human erythroid ankyrin Deposited 2008-11-03 Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain D 911–1068（158 aa） Fragment：ZU5-ANK, spectrin binding region of human erythroid ankyrin: UNP residues 911-1068
Not recorded BR BROMIDE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；20% PEG 4000, 0.25 M KBr, 10 mM DTT, 0.1 M MES pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.00 Å R-free 0.264
3KBT Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK) Deposited 2009-10-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 911–1068（158 aa） Fragment：UNP residues 911-1068
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；Protein complex at 7.5 mg/mL mixed 1:1 with 0.05 M MES pH 6.5, 0.2 M ammonium acetate, 0.01 M calcium chloride, 10% PEG-4000, 5 mM dithiothreitol, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.75 Å R-free 0.292
3KBT Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK) Deposited 2009-10-20 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 911–1068（158 aa） Fragment：UNP residues 911-1068
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；Protein complex at 7.5 mg/mL mixed 1:1 with 0.05 M MES pH 6.5, 0.2 M ammonium acetate, 0.01 M calcium chloride, 10% PEG-4000, 5 mM dithiothreitol, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.75 Å R-free 0.292
3KBU Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK), EMTS derivative Deposited 2009-10-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain D 911–1068（158 aa） Fragment：UNP residues 911-1068
Not recorded HG MERCURY (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；Protein complex at 7.5 mg/mL mixed 1:1 with 0.05 M MES pH 6.5, 0.2 M ammonium acetate, 0.01 M calcium chloride, 10% PEG-4000, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.75 Å R-free 0.277
3KBU Crystal structure of the ankyrin binding domain of human erythroid beta spectrin (repeats 13-15) in complex with the spectrin binding domain of human erythroid ankyrin (ZU5-ANK), EMTS derivative Deposited 2009-10-20 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 911–1068（158 aa） Fragment：UNP residues 911-1068
Not recorded HG MERCURY (II) ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；283 K；Protein complex at 7.5 mg/mL mixed 1:1 with 0.05 M MES pH 6.5, 0.2 M ammonium acetate, 0.01 M calcium chloride, 10% PEG-4000, VAPOR DIFFUSION, HANGING DROP, temperature 283K
Resolution 2.75 Å R-free 0.277
3UD1 Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 911–1233（323 aa） Fragment：ZU5A-ZU5B Ankyrin-R, UNP residues 911-1233
Not recorded EOH ETHANOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.00 Å R-free 0.206
3UD1 Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 911–1233（323 aa） Fragment：ZU5A-ZU5B Ankyrin-R, UNP residues 911-1233
Not recorded EOH ETHANOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.00 Å R-free 0.206
3UD1 Crystal structure of ZU5A-ZU5B domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 911–1233（323 aa） Fragment：ZU5A-ZU5B Ankyrin-R, UNP residues 911-1233
Not recorded EOH ETHANOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.00 Å R-free 0.206
3UD2 Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain C 911–1233（323 aa） Fragment：SeMet ZU5A-ZU5B Ankyrin-R,UNP residues 911-1233
Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 1 EOH ETHANOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.21 Å R-free 0.259
3UD2 Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 911–1233（323 aa） Fragment：SeMet ZU5A-ZU5B Ankyrin-R,UNP residues 911-1233
Non-standard monomer：Yes (specific site not provided by mmCIF) NA SODIUM ION × 16 EOH ETHANOL × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.21 Å R-free 0.259
3UD2 Crystal structure of Selenomethionine ZU5A-ZU5B protein domains of human erythrocyte ankyrin Deposited 2011-10-27 Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 911–1233（323 aa） Fragment：SeMet ZU5A-ZU5B Ankyrin-R,UNP residues 911-1233
Non-standard monomer：Yes (specific site not provided by mmCIF) EOH ETHANOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；283.15 K；25% ethanol, 0.1 M Tris pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 283.15K
Resolution 2.21 Å R-free 0.259
7TW3 Cryo-EM structure of human ankyrin complex (B2P1A1) from red blood cell Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain G 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
7TW5 Cryo-EM structure of human ankyrin complex (B2P1A2) from red blood cell Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain G 1–1881（1881 aa）
Chain H 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.70 Å
7TW6 Cryo-EM structure of human ankyrin complex (B4P1A1) from red blood cell Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain G 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 5.60 Å
7UZQ Local refinement of RhAG-RhCE-ANK1(AR1-5), from consensus refinement of all classes Deposited 2022-05-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain J 1–201（201 aa） Fragment：AR1-5 (UNP residues 1-201)
Not recorded CLR CHOLESTEROL × 2 AJP Digitonin × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL and 0.01% ( w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.17 Å
7UZU Ankyrin-1 (N-terminal region of membrane binding domain, local refinement from consensus reconstruction; bound to N-terminal peptide from band 3) Deposited 2022-05-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL and 0.01% ( w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.30 Å
7V0K Consensus refinement of human erythrocyte ankyrin-1 complex (Composite map) Deposited 2022-05-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain H 1–1881（1881 aa）
Not recorded CLR CHOLESTEROL × 6 AJP Digitonin × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PLC DIUNDECYL PHOSPHATIDYL CHOLINE × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.40 Å
7V0M Local refinement of ankyrin-1 (N-terminal half), class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.70 Å
7V0S Local refinement of RhAG/CE trimer, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain J 1–1881（1881 aa）
Not recorded CLR CHOLESTEROL × 2 AJP Digitonin × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.50 Å
7V0X Local refinement of ankyrin-1 (C-terminal half), class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-11 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain J 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds.
Resolution 3.00 Å
8CS9 Composite reconstruction of Class 1 of the erythrocyte ankyrin-1 complex Deposited 2022-05-12 Assembly 1 Other combination Heteromer；Protein × 18 PDB declaration: octadecameric（18） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded CLR CHOLESTEROL × 8 AJP Digitonin × 1 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.74 Å
8CSL Sub-tomogram averaging of erythrocyte ankyrin-1 complex Deposited 2022-05-12 Assembly 1 Protein heterocomplex Heteromer；Protein × 19 PDB declaration: nonadecameric（19） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；130 mM KCl, 10 mM HEPES, pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 25.00 Å
8CSV Local refinement of Anykyrin-1 (N-terminal half of membrane binding domain) in Class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.70 Å
8CTE Class 2 of erythrocyte ankyrin-1 complex (Composite map) Deposited 2022-05-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 14 PDB declaration: tetradecameric（14） Consistent with protein count
Chain A 1–1881（1881 aa）
Not recorded CLR CHOLESTEROL × 10 AJP Digitonin × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4；Final gel filtration buffer contained 0.05% w/v digitonin, 130 mM KCl, 20 mM HEPES, pH 7.4, 1 mM ATP, 1 mM MgCl2, 1 mM PMSF. Peak fractions were concentrated to 8 mg/mL, and 0.01% w/v glycyrrhizic acid was added immediately prior to vitrification.
cryo-EM vitrification conditions Cryogen ETHANE；4-6 seconds, wait time 30 seconds
Resolution 2.90 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.