PDBsum entry 5jqs

Hydrolase

PDB id: 5jqs

Contents

Protein chains

251 a.a.

75 a.a.

Ligands

AYE

SO4 ×3

DIO

Metals

_CL

Waters ×53

PDB id:

5jqs

Name:

Hydrolase

Title:

Crystal structure of deubiquitinase mindy-1 in complex with ubiquitin

Structure:

Protein fam63a. Chain: a. Engineered: yes. Ubiquitin-40s ribosomal protein s27a. Chain: d. Synonym: ubiquitin carboxyl extension protein 80. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fam63a, kiaa1390. Expressed in: escherichia coli. Expression_system_taxid: 562. Bos taurus. Bovine. Organism_taxid: 9913.

Resolution:

2.65Å R-factor: 0.207 R-free: 0.231

Authors:

S.A.Abdul Rehman,Y.Kulathu

Key ref:

S.A.Abdul Rehman et al. (2016). MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes. Mol Cell, 63, 146-155. PubMed id: 27292798 DOI: 10.1016/j.molcel.2016.05.009

Date:

05-May-16 Release date: 22-Jun-16

Protein chain

Q8N5J2  (MINY1_HUMAN) -  Ubiquitin carboxyl-terminal hydrolase MINDY-1 from Homo sapiens

Seq: 469 a.a.

Struc: 251 a.a.

Protein chain

P62992  (RS27A_BOVIN) -  Ubiquitin-ribosomal protein eS31 fusion protein from Bos taurus

Seq: 156 a.a.

Struc: 75 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.3.4.19.12 - ubiquitinyl hydrolase 1.
• Reaction: Thiol-dependent hydrolysis of ester, thiolester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).

DOI no: 10.1016/j.molcel.2016.05.009

Mol Cell 63:146-155 (2016)

PubMed id: 27292798

MINDY-1 Is a Member of an Evolutionarily Conserved and Structurally Distinct New Family of Deubiquitinating Enzymes.

S.A.Abdul Rehman, Y.A.Kristariyanto, S.Y.Choi, P.J.Nkosi, S.Weidlich, K.Labib, K.Hofmann, Y.Kulathu.

ABSTRACT

No abstract given.