Uniprot accession / id : Q3U2S4  OR   Uniprot accession / id : Q96G74
 
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revised
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Entry Information
Entry status  (1)
REL
(3)
 
Experimental methods  (1)
X-ray diffraction
(3)
 
Authors  (26)
Arnott D
(2)
Bosanac I
(2)
Cochran A
(2)
Cochran AG
(2)
Dixit VM
(2)
Flinders J
(2)
Huang OW
(2)
Hymowitz S
(2)
Hymowitz SG
(2)
Kayagaki N
(2)
Ma X
(2)
Maurer T
(2)
Phung Q
(2)
Starovasnik M
(2)
Starovasnik MA
(2)
Yin J
(2)
Arrowsmith CH
(1)
Asinas AE
(1)
Bountra C
(1)
Crombet L
(1)
Dhe-Paganon S
(1)
Dong A
(1)
Edwards AM
(1)
Structural Genomics Consortium (SGC)
(1)
Walker JR
(1)
Weigelt J
(1)
 
Homo / hetero assembly  (2)
homo
(2)
hetero
(1)
 
Assembly composition  (2)
protein structure
(2)
protein/protein complex
(1)
 
Assembly polymer count  (2)
monomer
(2)
dimer
(1)
 
Resolution distribution
1.5 - 2
(2)
2.0 - 2.5
(1)
 
Release year distribution
2005 - 2010
(1)
2010 - 2015
(3)
 
Journal  (2)
Nat Struct Mol Biol
(2)
To be published
(1)
 
Macromolecules
Organism superkingdom  (1)
Eukaryota
(3)
 
Organism name  (1)
Homo sapiens
(3)
 
Molecule name  (3)
DUBA
(3)
Deubiquitinating enzyme A
(3)
OTU domain-containing protein 5
(3)
 
Molecule type  (1)
Protein
(3)
 
Gene names  (1)
OTUD5
(3)
 
Interacting Molecules  (1)
Ubiquitin
(1)
 
Interacting ligands  (3)
PEG : DI(HYDROXYETHYL)ETHER
(1)
PG4 : TETRAETHYLENE GLYCOL
(1)
SO4 : SULFATE ION
(1)
 
Function and Biology
EC number / name  (1)
3.4.19.12 : Ubiquitinyl hydrolase 1
(3)
 
Sequence and Structure classification
CATH class  (2)
Alpha Beta
(3)
Special
(2)
 
CATH topology  (3)
Arc Repressor Mutant, subunit A
(2)
Phosphorylase Kinase; domain 1
(2)
Cathepsin B; Chain A
(1)
 
Pfam accession / name  (1)
PF02338 : OTU
(3)
 
Experimental Information
Diffraction protocol  (2)
Single wavelength
(2)
MAD
(1)
 
Diffraction radiation source type  (1)
Synchrotron
(3)
 
Diffraction source  (3)
APS BEAMLINE 21-ID-G
(1)
APS BEAMLINE 23-ID-D
(1)
ESRF BEAMLINE ID29
(1)
 
Synchrotron site  (2)
APS
(2)
ESRF
(1)
 
Diffraction detector type  (1)
CCD
(3)
 
Refinement software  (1)
REFMAC
(3)
 
Representative Structures
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Entries 1 to 3 of 3
Entries 1 to 3 of 3
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The catalytic domain of human deubiquitinase DUBA in complex with ubiquitin aldehyde
Ma X, Yin J, Hymowitz S, Starovasnik M, Cochran A
Nat Struct Mol Biol (2012) [PMID: 22245969  ]
Source organism: Homo sapiens  
Assembly composition: protein/protein complex
Modified residues: SEP    GLZ    GLZ    SEP   
Assembly name: Ubiquitin and OTU domain-containing protein 5 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-143397 (Preferred)   search this ID
PDBe-KB: Q96G74    P0CG48   
X-ray diffraction
1.91Å resolution
Released: 11 Jan 2012
Model geometry
Fit model/data
3tmp
3tmp
3tmp
The catalytic domain of human OTUD5
Walker JR, Asinas AE, Crombet L, Dong A, Weigelt J, Bountra C, Arrowsmith CH, Edwards AM, Dhe-Paganon S, Structural Genomics Consortium (SGC)
To be published
Source organism: Homo sapiens  
Assembly composition: protein only structure
Bound ligands: PEG    PG4    PEG    SO4    PG4   
Modified residues: MSE    MSE   
Assembly name: OTU domain-containing protein 5 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-188512 (Preferred)   search this ID
PDBe-KB: Q96G74    Q96G74   
X-ray diffraction
1.702Å resolution
Released: 15 Dec 2010
Model geometry
Fit model/data
3pfy
3pfy
3pfy
The catalytic domain of human deubiquitinase DUBA
Yin J, Bosanac I, Ma X, Hymowitz S, Starovasnik M, Cochran A
Nat Struct Mol Biol (2012) [PMID: 22245969  ]
Source organism: Homo sapiens  
Assembly composition: protein only structure
Modified residues: MSE    MSE   
Assembly name: OTU domain-containing protein 5 (Preferred)   search this complex
PDBe complex ID: PDB-CPX-188512 (Preferred)   search this ID
PDBe-KB: Q96G74   
X-ray diffraction
2.2Å resolution
Released: 11 Jan 2012
Model geometry
Fit model/data
3tmo
3tmo
3tmo
Entries 1 to 3 of 3
Entries 1 to 3 of 3