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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：Q51911 New Search
12PDB entries
13Biological assembly
13chain/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
1GAB STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES Deposited 1996-12-30 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213 - 265
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K
Resolution not provided
1PRB STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1997-01-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213 - 265
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K
Resolution not provided
1TF0 Crystal structure of the GA module complexed with human serum albumin Deposited 2004-05-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 213–265（53 aa）
Not recorded DKA DECANOIC ACID × 3 CIT CITRIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；Ammonium sulfate, citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.70 Å R-free 0.295
2J5Y Crystal structure of the GA module from F.magna Deposited 2006-09-20 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213-265
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；22-26% (W/V) PEG 3350, 50 MM POTASSIUM PHOSPHATE PH 7.5, 100 MM AMMONIUM ACETATE
Resolution 1.40 Å R-free 0.199
2J5Y Crystal structure of the GA module from F.magna Deposited 2006-09-20 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 213–265（53 aa） Fragment：ALBUMIN-BINDING DOMAIN, RESIDUES 213-265
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；22-26% (W/V) PEG 3350, 50 MM POTASSIUM PHOSPHATE PH 7.5, 100 MM AMMONIUM ACETATE
Resolution 1.40 Å R-free 0.199
2VDB Structure of human serum albumin with S-naproxen and the GA module Deposited 2007-10-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 213–265（53 aa） Fragment：RESIDUES 213-265
Not recorded DKA DECANOIC ACID × 6 NPS (2S)-2-(6-methoxynaphthalen-2-yl)propanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions 26-32% PEG 3350, 50 MM POTASSIUM PHOSPHATE, 0.1 M AMMONIUM PHOSPHATE/POTASSIUM PHOSPHATE
Resolution 2.52 Å R-free 0.280
9BB1 Backbone Modification in the GA Module of Protein PAB: Wild-type Sequence Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB2 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 20 and 24 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 20 and 24, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB3 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 22 and 26 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 22 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB4 Backbone Modification in the GA Module of Protein PAB: beta3-residues at positions 23 and 26 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: beta3 residues at positions 23 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB5 Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 22 and 26 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.9；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: ACPC residues at positions 22 and 26, 0.2 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB6 Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.8；283 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 1 mM GA Module of Protein PAB: ACPC residues at positions 5 and 13, beta3 residue at position 9, 0.2 mM dss, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
9BB7 Backbone Modification in the GA Module of Protein PAB: ACPC residues at positions 5 and 39, beta3 residue at position 26 Deposited 2024-04-05 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 219–265（47 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5.6；300 K；Ionic strength (raw mmCIF value) 1；Pressure 1
NMR sample composition 0.88 mM GA Module of Protein PAB: ACPC residues at positions 5 and 39, beta3 residue at position 26, 0.19 mM DSS, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided

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.