PDBsum entry 3dd3

Transferase

PDB id: 3dd3

Contents

Protein chain

210 a.a. *

Ligands

MES ×2

RUC

GSH ×2

Waters ×74

* Residue conservation analysis

PDB id:

3dd3

Name:

Transferase

Title:

Crystal structure of the glutathione transferase pi enzyme in complex with the bifunctional inhibitor, etharapta

Structure:

Glutathione s-transferase p. Chain: a, b. Synonym: gst class-pi, gstp1-1, glutathione transferase pi. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: gstp1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.25Å R-factor: 0.200 R-free: 0.260

Authors:

L.J.Parker

Key ref:

W.H.Ang et al. (2009). Rational design of an organometallic glutathione transferase inhibitor. Angew Chem Int Ed Engl, 48, 3854-3857. PubMed id: 19396894

Date:

05-Jun-08 Release date: 21-Apr-09

Protein chains

P09211  (GSTP1_HUMAN) -  Glutathione S-transferase P from Homo sapiens

Seq: 210 a.a.

Struc: 210 a.a.

Enzyme reactions

• Enzyme class: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

RX (Bound ligand (Het Group name = GSH) corresponds exactly) + glutathione = S-substituted glutathione + halide anion + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Angew Chem Int Ed Engl 48:3854-3857 (2009)

PubMed id: 19396894

Rational design of an organometallic glutathione transferase inhibitor.

W.H.Ang, L.J.Parker, A.De Luca, L.Juillerat-Jeanneret, C.J.Morton, M.Lo Bello, M.W.Parker, P.J.Dyson.

ABSTRACT

Double trouble: A hybrid organic-inorganic (organometallic) inhibitor was designed to target glutathione transferases. The metal center is used to direct protein binding, while the organic moiety acts as the active-site inhibitor (see picture). The mechanism of inhibition was studied using a range of biophysical and biochemical methods.