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PDBsum entry 4dhz
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Hydrolase/signaling protein/ligase
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PDB id
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4dhz
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Contents |
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256 a.a.
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76 a.a.
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72 a.a.
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149 a.a.
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PDB id:
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| Name: |
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Hydrolase/signaling protein/ligase
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Title:
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The structure of h/ceotub1-ubiquitin aldehyde-ubc13~ub
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Structure:
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Ubiquitin thioesterase otubain-like. Chain: a. Fragment: see remark 999. Synonym: deubiquitinating enzyme otub1, otu domain-containing ubiquitin aldehyde-binding protein 1, otubain-1, hotu1, ubiquitin- specific-processing protease otub1, deubiquitinating enzyme otubain- like, ubiquitin-specific-processing protease otubain-like. Engineered: yes. Ubiquitin aldehyde.
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Source:
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Homo sapiens, caenorhabditis elegans. Human, nematode. Organism_taxid: 9606, 6239. Gene: otub1, otb1, otu1, hspc263, c25d7.8, otub-1. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.
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Resolution:
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3.11Å
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R-factor:
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0.236
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R-free:
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0.288
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Authors:
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R.Wiener,X.Zhang,T.Wang,C.Wolberger
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Key ref:
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R.Wiener
et al.
(2012).
The mechanism of OTUB1-mediated inhibition of ubiquitination.
Nature,
483,
618-622.
PubMed id:
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Date:
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30-Jan-12
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Release date:
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22-Feb-12
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PROCHECK
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Headers
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References
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Q96FW1
(OTUB1_HUMAN) -
Ubiquitin thioesterase OTUB1 from Homo sapiens
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Seq:
Struc:
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271 a.a.
256 a.a.*
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Q9XVR6
(OTUBL_CAEEL) -
Ubiquitin thioesterase otubain-like from Caenorhabditis elegans
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Seq:
Struc:
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284 a.a.
256 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 2:
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Chain A:
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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Enzyme class 3:
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Chain F:
E.C.2.3.2.23
- E2 ubiquitin-conjugating enzyme.
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Reaction:
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L- cysteine
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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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Nature
483:618-622
(2012)
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PubMed id:
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The mechanism of OTUB1-mediated inhibition of ubiquitination.
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R.Wiener,
X.Zhang,
T.Wang,
C.Wolberger.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Ye,
G.Blaser,
M.H.Horrocks,
M.J.Ruedas-Rama,
S.Ibrahim,
A.A.Zhukov,
A.Orte,
D.Klenerman,
S.E.Jackson,
and
D.Komander
(2012).
Ubiquitin chain conformation regulates recognition and activity of interacting proteins.
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Nature,
492,
266-270.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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