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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：P16452 New Search
13PDB entries
13Biological assembly
14chain/assembly records
Main Difference Dimensions in This Set
Different assembly state Different ligand/ion 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
7TVZ Cryo-EM structure of human band 3-protein 4.2 complex in diagonal conformation Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain E 1–691（691 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 LMT DODECYL-BETA-D-MALTOSIDE × 5 CLR CHOLESTEROL × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
7TW0 Cryo-EM structure of human band 3-protein 4.2 complex in vertical conformation Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain E 1–691（691 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.60 Å
7TW1 Cryo-EM structure of human band 3-protein 4.2 complex (B2P2vertical) Deposited 2022-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 1–691（691 aa）
Chain F 1–691（691 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.60 Å
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 E 1–691（691 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 E 1–691（691 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 E 1–691（691 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
7UZS Protein 4.2 (local refinement from consensus reconstruction of ankyrin complex classes) Deposited 2022-05-09 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain X 1–691（691 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 2.20 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 X 1–691（691 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
7V0Q Local refinement of protein 4.2, class 1 of erythrocyte ankyrin-1 complex Deposited 2022-05-10 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain X 1–691（691 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 2.50 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 X 1–691（691 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 X 1–691（691 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
8CSW Local refinement of protein 4.2 in Class 2 of erythrocyte ankyrin-1 complex Deposited 2022-05-13 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain X 1–691（691 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 2.50 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 X 1–691（691 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.