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PDBsum entry 4dhj

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protein Protein-protein interface(s) links
Hydrolase/signaling protein/ligase PDB id
4dhj

 

 

 

 

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Contents
Protein chains
248 a.a.
76 a.a.
71 a.a.
149 a.a.
Waters ×309
PDB id:
4dhj
Name: Hydrolase/signaling protein/ligase
Title: The structure of a ceotub1 ubiquitin aldehyde ubc13~ub complex
Structure: Ubiquitin thioesterase otubain-like. Chain: a, e, i, l. Synonym: otub1, deubiquitinating enzyme otubain-like, ubiquitin- specific-processing protease otubain-like. Engineered: yes. Ubiquitin aldehyde. Chain: b, f, j, m. Engineered: yes. Ubiquitin.
Source: Caenorhabditis elegans. Nematode. Organism_taxid: 6239. Gene: otub-1, c25d7.8. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.
Resolution:
2.35Å     R-factor:   0.204     R-free:   0.237
Authors: R.Wiener,X.Zhang,T.Wang,C.Wolberger
Key ref: R.Wiener et al. (2012). The mechanism of OTUB1-mediated inhibition of ubiquitination. Nature, 483, 618-622. PubMed id: 22367539
Date:
27-Jan-12     Release date:   22-Feb-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9XVR6  (OTUBL_CAEEL) -  Ubiquitin thioesterase otubain-like from Caenorhabditis elegans
Seq:
Struc:
284 a.a.
248 a.a.
Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
76 a.a.*
Protein chains
Pfam   ArchSchema ?
P0CG48  (UBC_HUMAN) -  Polyubiquitin-C from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
685 a.a.
71 a.a.
Protein chains
Pfam   ArchSchema ?
P61088  (UBE2N_HUMAN) -  Ubiquitin-conjugating enzyme E2 N from Homo sapiens
Seq:
Struc:
152 a.a.
149 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: Chains A, E, I, L: E.C.3.4.19.12  - ubiquitinyl hydrolase 1.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 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).
   Enzyme class 3: Chains C, K, G, N: E.C.2.3.2.23  - E2 ubiquitin-conjugating enzyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 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
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.

 

 
Nature 483:618-622 (2012)
PubMed id: 22367539  
 
 
The mechanism of OTUB1-mediated inhibition of ubiquitination.
R.Wiener, X.Zhang, T.Wang, C.Wolberger.
 
  ABSTRACT  
 
No abstract given.

 

Literature references that cite this PDB file's key reference

  PubMed id Reference
23201676 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.
  Nature, 492, 266-270.  
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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