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PDBsum entry 3tmp
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Hydrolase/protein binding
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PDB id
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3tmp
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Contents |
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166 a.a.
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76 a.a.
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168 a.a.
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154 a.a.
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PDB id:
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| Name: |
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Hydrolase/protein binding
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Title:
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The catalytic domain of human deubiquitinase duba in complex with ubiquitin aldehyde
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Structure:
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Otu domain-containing protein 5. Chain: a, c, e, g. Fragment: catalytic or otu domain (residues 172-351). Synonym: deubiquitinating enzyme a, duba. Engineered: yes. Mutation: yes. Polyubiquitin-c. Chain: b, d, f, h. Fragment: ubiquitin-like 1.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: duba, otud5. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: ubc, ubiquitin aldehyde. Expression_system_taxid: 562
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Resolution:
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1.91Å
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R-factor:
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0.192
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R-free:
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0.227
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Authors:
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X.Ma,J.Yin,S.Hymowitz,M.Starovasnik,A.Cochran
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Key ref:
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O.W.Huang
et al.
(2012).
Phosphorylation-dependent activity of the deubiquitinase DUBA.
Nat Struct Biol,
19,
171-175.
PubMed id:
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Date:
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31-Aug-11
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Release date:
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11-Jan-12
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PROCHECK
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Headers
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References
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Q96G74
(OTUD5_HUMAN) -
OTU domain-containing protein 5 from Homo sapiens
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Seq:
Struc:
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571 a.a.
166 a.a.
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P0CG48
(UBC_HUMAN) -
Polyubiquitin-C from Homo sapiens
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Seq:
Struc:
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685 a.a.
76 a.a.*
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Enzyme class:
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Chains A, C, E, G:
E.C.3.4.19.12
- ubiquitinyl hydrolase 1.
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Reaction:
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Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
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Nat Struct Biol
19:171-175
(2012)
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PubMed id:
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Phosphorylation-dependent activity of the deubiquitinase DUBA.
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O.W.Huang,
X.Ma,
J.Yin,
J.Flinders,
T.Maurer,
N.Kayagaki,
Q.Phung,
I.Bosanac,
D.Arnott,
V.M.Dixit,
S.G.Hymowitz,
M.A.Starovasnik,
A.G.Cochran.
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ABSTRACT
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Links
