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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：Q96G74 New Search
3PDB entries
7Biological assembly
7chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification 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
3PFY The catalytic domain of human OTUD5 Deposited 2010-10-29 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 172–339（168 aa） Fragment：OTU DOMAIN (UNP Residues 172-339)
Non-standard monomer：Yes (specific site not provided by mmCIF) PEG DI(HYDROXYETHYL)ETHER × 2 PG4 TETRAETHYLENE GLYCOL × 1 SO4 SULFATE ION × 1 UNX UNKNOWN LIGAND × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；2% PEG 400, 2 M AMMONIUM SULFATE, 0.1 M SODIUM HEPES, PH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 1.70 Å R-free 0.207
3TMO The catalytic domain of human deubiquitinase DUBA Deposited 2011-08-31 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：3.4.19.12 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, SITTING DROP；pH 7；293 K；0.8 M succinic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.276
3TMO The catalytic domain of human deubiquitinase DUBA Deposited 2011-08-31 Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：3.4.19.12 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, SITTING DROP；pH 7；293 K；0.8 M succinic acid, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.20 Å R-free 0.276
3TMP The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde Deposited 2011-08-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：S172 phosphorylated 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, SITTING DROP；pH 5.8；293 K；20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.91 Å R-free 0.227
3TMP The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde Deposited 2011-08-31 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain C 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：S172 phosphorylated 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, SITTING DROP；pH 5.8；293 K；20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.91 Å R-free 0.227
3TMP The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde Deposited 2011-08-31 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：S172 phosphorylated 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, SITTING DROP；pH 5.8；293 K；20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.91 Å R-free 0.227
3TMP The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde Deposited 2011-08-31 Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 172–351（180 aa） Fragment：catalytic or OTU domain (Residues 172-351)
Mutation：S172 phosphorylated 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, SITTING DROP；pH 5.8；293 K；20% PEG3350, 0.2 M Ammonium Fluoride, and 0.1M Bis-Tris, pH 5.8, VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 1.91 Å R-free 0.227

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.