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PDBsum entry 1yla

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protein Protein-protein interface(s) links
Ligase PDB id
1yla

 

 

 

 

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Contents
Protein chains
201 a.a. *
Waters ×150
* Residue conservation analysis
PDB id:
1yla
Name: Ligase
Title: Ubiquitin-conjugating enzyme e2-25 kda (huntington interacting protein 2)
Structure: Ubiquitin-conjugating enzyme e2-25 kda. Chain: a, b. Synonym: ubiquitin- protein ligase, ubiquitin carrier protein, e225k, huntingtin interacting protein 2, hip-2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hip2, lig. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.40Å     R-factor:   0.225     R-free:   0.269
Authors: J.Choe,G.V.Avvakumov,E.M.Newman,F.Mackenzie,I.Kozieradzki, A.Bochkarev,M.Sundstrom,C.Arrowsmith,A.Edwards,S.Dhe-Paganon, Structural Genomics Consortium (Sgc)
Key ref: S.Ko et al. (2010). Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity. J Biol Chem, 285, 36070-36080. PubMed id: 20826778
Date:
19-Jan-05     Release date:   01-Feb-05    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P61086  (UBE2K_HUMAN) -  Ubiquitin-conjugating enzyme E2 K from Homo sapiens
Seq:
Struc:
200 a.a.
201 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: 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

 

 
J Biol Chem 285:36070-36080 (2010)
PubMed id: 20826778  
 
 
Structural basis of E2-25K/UBB+1 interaction leading to proteasome inhibition and neurotoxicity.
S.Ko, G.B.Kang, S.M.Song, J.G.Lee, D.Y.Shin, J.H.Yun, Y.Sheng, C.Cheong, Y.H.Jeon, Y.K.Jung, C.H.Arrowsmith, G.V.Avvakumov, S.Dhe-Paganon, Y.J.Yoo, S.H.Eom, W.Lee.
 
  ABSTRACT  
 
No abstract given.

 

 

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