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PDBsum entry 1y6l

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protein Protein-protein interface(s) links
Ligase PDB id
1y6l
Jmol
Contents
Protein chains
148 a.a. *
Waters ×369
* Residue conservation analysis
PDB id:
1y6l
Name: Ligase
Title: Human ubiquitin conjugating enzyme e2e2
Structure: Ubiquitin-conjugating enzyme e2e2. Chain: a, b, c. Fragment: residues 55-201. Synonym: ubiquitin-protein ligase e2, ubiquitin carrier pro ubch8. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ube2e2, ubch8. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.194     R-free:   0.246
Authors: J.R.Walker,G.V.Avvakumov,E.M.Newman,F.Mackenzie,I.Kozieradzk A.Bochkarev,M.Sundstrom,C.Arrowsmith,A.Edwards,S.Dhe-Pagano Structural Genomics Consortium (Sgc)
Key ref: Y.Sheng et al. (2012). A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen. Mol Cell Proteomics, 11, 329-341. PubMed id: 22496338 DOI: 10.1074/mcp.O111.013706
Date:
06-Dec-04     Release date:   11-Jan-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
No UniProt id for this chain
Struc: 148 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.6.3.2.19  - Ubiquitin--protein ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine
ATP
+ ubiquitin
+ protein lysine
= AMP
+ diphosphate
+ protein N-ubiquityllysine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     acid-amino acid ligase activity     1 term  

 

 
    reference    
 
 
DOI no: 10.1074/mcp.O111.013706 Mol Cell Proteomics 11:329-341 (2012)
PubMed id: 22496338  
 
 
A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen.
Y.Sheng, J.H.Hong, R.Doherty, T.Srikumar, J.Shloush, G.V.Avvakumov, J.R.Walker, S.Xue, D.Neculai, J.W.Wan, S.K.Kim, C.H.Arrowsmith, B.Raught, S.Dhe-Paganon.
 
  ABSTRACT  
 
No abstract given.