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PDBsum entry 3zjf
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PDB id:
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Hydrolase
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Title:
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A20 otu domain with irreversibly oxidised cys103 from 270 min h2o2 soak.
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Structure:
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A20p50. Chain: a. Fragment: otu domain, residues 1-366. Synonym: tumor necrosis factor alpha-induced protein 3, tnf alpha- induced protein 3, otu domain-containing protein 7c, putative DNA- binding protein a20, zinc finger protein a20, a20. Engineered: yes. Mutation: yes. Other_details: the catalytic cys103 is irreversibly oxidised and
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.20Å
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R-factor:
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0.184
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R-free:
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0.222
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Authors:
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Y.Kulathu,F.J.Garcia,T.E.T.Mevissen,M.Busch,N.Arnaudo,K.S.Carroll, D.Barford,D.Komander
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Key ref:
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Y.Kulathu
et al.
(2013).
Regulation of A20 and other OTU deubiquitinases by reversible oxidation.
Nat Commun,
4,
1569.
PubMed id:
DOI:
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Date:
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17-Jan-13
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Release date:
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06-Mar-13
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PROCHECK
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Headers
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References
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P21580
(TNAP3_HUMAN) -
Tumor necrosis factor alpha-induced protein 3 from Homo sapiens
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Seq:
Struc:
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790 a.a.
323 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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Enzyme class 1:
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E.C.2.3.2.-
- ?????
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Enzyme class 2:
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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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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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DOI no:
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Nat Commun
4:1569
(2013)
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PubMed id:
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Regulation of A20 and other OTU deubiquitinases by reversible oxidation.
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Y.Kulathu,
F.J.Garcia,
T.E.Mevissen,
M.Busch,
N.Arnaudo,
K.S.Carroll,
D.Barford,
D.Komander.
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ABSTRACT
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Links
