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PDBsum entry 2lbc
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PDB id:
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Hydrolase
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Title:
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Solution structure of tandem uba of usp13
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Structure:
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Ubiquitin carboxyl-terminal hydrolase 13. Chain: a. Fragment: unp residues 652-777. Synonym: deubiquitinating enzyme 13, isopeptidase t-3, isot-3, ubiquitin thiolesterase 13, ubiquitin-specific-processing protease 13. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: usp13, isot3. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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15 models
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Authors:
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Y.Zhang,C.Zhou,Z.Zhou,A.Song,H.Hu
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Key ref:
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Y.H.Zhang
et al.
(2011).
Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.
Plos One,
6,
e29362.
PubMed id:
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Date:
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29-Mar-11
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Release date:
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07-Mar-12
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PROCHECK
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Headers
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References
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Q92995
(UBP13_HUMAN) -
Ubiquitin carboxyl-terminal hydrolase 13 from Homo sapiens
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Seq:
Struc:
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863 a.a.
126 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Enzyme class:
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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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Plos One
6:e29362
(2011)
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PubMed id:
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Domain analysis reveals that a deubiquitinating enzyme USP13 performs non-activating catalysis for Lys63-linked polyubiquitin.
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Y.H.Zhang,
C.J.Zhou,
Z.R.Zhou,
A.X.Song,
H.Y.Hu.
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ABSTRACT
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