PDBsum entry 3l11

Ligase

PDB id: 3l11

Contents

Protein chain

104 a.a. *

Ligands

MLI ×2

Metals

_ZN ×2

Waters ×34

* Residue conservation analysis

PDB id:

3l11

Name:

Ligase

Title:

Crystal structure of the ring domain of rnf168

Structure:

E3 ubiquitin-protein ligase rnf168. Chain: a. Fragment: ring domain (unp residues 1-113). Synonym: ring finger protein 168. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: bc033791, rnf168. Expressed in: escherichia coli. Expression_system_taxid: 469008.

Resolution:

2.12Å R-factor: 0.189 R-free: 0.215

Authors:

D.Neculai,L.Yermekbayeva,L.Crombet,J.Weigelt,C.Bountra,A.M.Edwards, C.H.Arrowsmith,A.Bochkarev,S.Dhe-Paganon,Structural Genomics Consortium (Sgc)

Key ref:

S.J.Campbell et al. (2012). Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation. J Biol Chem, 287, 23900-23910. PubMed id: 22589545

Date:

10-Dec-09 Release date: 19-Jan-10

Protein chain

Q8IYW5  (RN168_HUMAN) -  E3 ubiquitin-protein ligase RNF168 from Homo sapiens

Seq: 571 a.a.

Struc: 104 a.a.

Enzyme reactions

• Enzyme class: E.C.2.3.2.27 - RING-type E3 ubiquitin transferase.
• Reaction: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N₆- ubiquitinyl-[acceptor protein]-L-lysine

J Biol Chem 287:23900-23910 (2012)

PubMed id: 22589545

Molecular insights into the function of RING finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.

S.J.Campbell, R.A.Edwards, C.C.Leung, D.Neculai, C.D.Hodge, S.Dhe-Paganon, J.N.Glover.

ABSTRACT

No abstract given.