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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：P54253 New Search
6PDB entries
12Biological assembly
18chain/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
1OA8 AXH domain of human spinocerebellar ataxin-1 Deposited 2003-01-02 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694
Chain B 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694
Not recorded NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；290 K；PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS/HCL, PH 7.0, 0.2M AMMONIUM SULPHATE, 5 MM DTT, 15% PEG 4000, 20% GLYCEROL, AT 290K
Resolution 1.70 Å R-free 0.252
1OA8 AXH domain of human spinocerebellar ataxin-1 Deposited 2003-01-02 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694
Chain D 563–694（132 aa） Fragment：AXH DOMAIN, RESIDUES 562-694
Not recorded NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；290 K；PROTEIN WAS CRYSTALLIZED FROM 0.1M TRIS/HCL, PH 7.0, 0.2M AMMONIUM SULPHATE, 5 MM DTT, 15% PEG 4000, 20% GLYCEROL, AT 290K
Resolution 1.70 Å R-free 0.252
2M41 Solution Structure of the AXH domain of Ataxin-1 in complex with ligand peptide from Capicua Deposited 2013-01-28 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 566–688（123 aa） Fragment：AXH domain, native residues A567-K689
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；310 K；Ionic strength (raw mmCIF value) 20；Pressure ambient
NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-100% 15N] Ataxin-1 AXH domain, 0.6 mM CIC polypeptide, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
4APT The structure of the AXH domain of ataxin-1. Deposited 2012-04-05 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Chain B 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.4 M POTASSIUM SODIUM TARTRATE AT ROOM TEMPERATURE.
Resolution 2.50 Å R-free 0.288
4APT The structure of the AXH domain of ataxin-1. Deposited 2012-04-05 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Chain D 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Not recorded NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.4 M POTASSIUM SODIUM TARTRATE AT ROOM TEMPERATURE.
Resolution 2.50 Å R-free 0.288
4AQP The structure of the AXH domain of ataxin-1. Deposited 2012-04-19 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Chain B 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Not recorded NA SODIUM ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.1 M MES, PH 6.5, 10% W/V PWG 20000 AT ROOM TEMPERATURE.
Resolution 2.45 Å R-free 0.267
4AQP The structure of the AXH domain of ataxin-1. Deposited 2012-04-19 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Chain D 566–688（123 aa） Fragment：AXH DOMAIN, RESIDUES 566-688
Not recorded NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；PROTEIN SAMPLES AT 20 MG/ML CRYSTALLISED IN 0.1 M MES, PH 6.5, 10% W/V PWG 20000 AT ROOM TEMPERATURE.
Resolution 2.45 Å R-free 0.267
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688
Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.270
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688
Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.270
4J2J Crystal structure of AXH domain complex with Capicua Deposited 2013-02-04 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688
Mutation：I580M,I605M Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；0.1M Calcium chloride, 24%(v/v) PEG3350, 4%(v/v) pentaerythritol ethoxylate, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.270
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.15 Å R-free 0.294
4J2L Crystal Structure of AXH domain complexed with Capicua Deposited 2013-02-04 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 562–688（127 aa） Fragment：AXH domain, UNP residues 562-688
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；293 K；1.6M NaCl, 3%(v/v) glycerol, 16%(w/v) PEG3350, 1mM L-Glutathione, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.15 Å R-free 0.294

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.