PDBsum entry: 1yla

Ligase

PDB id: 1yla

Contents

Protein chains

201 a.a. *

Waters ×150

* Residue conservation analysis

PDB id:

1yla

Name:

Ligase

Title:

Ubiquitin-conjugating enzyme e2-25 kda (huntington interacti 2)

Structure:

Ubiquitin-conjugating enzyme e2-25 kda. Chain: a, b. Synonym: ubiquitin- protein ligase, ubiquitin carrier prote 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-Pagano 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 DOI: 10.1074/jbc.M110.145219

Date:

19-Jan-05 Release date: 01-Feb-05

Protein chains

P61086  (UBE2K_HUMAN) -  Ubiquitin-conjugating enzyme E2 K

Seq: 200 a.a.

Struc: 201 a.a.

Enzyme reactions

• Enzyme class: E.C.6.3.2.19 - Ubiquitin--protein ligase.
• Reaction: 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 

• Cellular component: cytoplasm (1 term)
• Biological process: regulation of protein metabolic process (4 terms)
• Biochemical function: nucleotide binding (8 terms)

reference

DOI no: 10.1074/jbc.M110.145219

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.