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PDBsum entry 2ob4

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protein links
Ligase PDB id
2ob4
Jmol
Contents
Protein chain
157 a.a. *
Waters ×70
* Residue conservation analysis
PDB id:
2ob4
Name: Ligase
Title: Human ubiquitin-conjugating enzyme cdc34
Structure: Ubiquitin-conjugating enzyme e2-32 kda complement chain: a. Fragment: catalytic domain: residues 7-184. Synonym: ubiquitin-protein ligase, ubiquitin carrier protei cdc34. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: cdc34, ube2r1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.40Å     R-factor:   0.226     R-free:   0.284
Authors: D.Neculai,G.V.Avvakumov,S.Xue,J.R.Walker,F.Mackenzie,J.Weige M.Sundstrom,C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,F.Sicher Paganon,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:
18-Dec-06     Release date:   26-Dec-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P49427  (UB2R1_HUMAN) -  Ubiquitin-conjugating enzyme E2 R1
Seq:
Struc:
236 a.a.
157 a.a.
Key:    PfamA domain  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

 

 
    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.