PDBsum entry 3q49

Ligase/chaperone

PDB id: 3q49

Contents

Protein chain

132 a.a.

Ligands

PRO-THR-ILE-GLU-GLU-VAL-ASP

Waters ×197

PDB id:

3q49

Name:

Ligase/chaperone

Title:

Crystal structure of the tpr domain of chip complexed with hsp70-c peptide

Structure:

Stip1 homology and u box-containing protein 1. Chain: b. Fragment: tpr domain. Synonym: carboxy terminus of hsp70-interacting protein, e3 ubiquitin- protein ligase chip. Engineered: yes. Hsp70-c peptide. Chain: c. Engineered: yes

Source:

Mus musculus. Mouse. Organism_taxid: 10090. Gene: stub1, chip. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Homo sapiens. Human.

Resolution:

1.54Å R-factor: 0.170 R-free: 0.207

Authors:

L.Wang,L.Chen,J.W.Wu

Key ref:

L.Wang et al. (2011). Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP). J Biol Chem, 286, 15883-15894. PubMed id: 21454478

Date:

23-Dec-10 Release date: 16-Mar-11

Protein chain

Q9WUD1  (CHIP_MOUSE) -  E3 ubiquitin-protein ligase CHIP from Mus musculus

Seq: 304 a.a.

Struc: 132 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 286:15883-15894 (2011)

PubMed id: 21454478

Molecular mechanism of the negative regulation of Smad1/5 protein by carboxyl terminus of Hsc70-interacting protein (CHIP).

L.Wang, Y.T.Liu, R.Hao, L.Chen, Z.Chang, H.R.Wang, Z.X.Wang, J.W.Wu.

ABSTRACT

No abstract given.