PDBsum entry 2wpe

Oxidoreductase

PDB id: 2wpe

Contents

Protein chains

490 a.a. *

Ligands

FAD ×4

WPE ×4

MPD

MRD

Metals

_CL ×18

_NA ×4

Waters ×1216

* Residue conservation analysis

PDB id:

2wpe

Name:

Oxidoreductase

Title:

Trypanosoma brucei trypanothione reductase in complex with 3,4- dihydroquinazoline inhibitor (ddd00073359)

Structure:

Trypanothione reductase. Chain: a, b, c, d. Engineered: yes

Source:

Trypanosoma brucei. Organism_taxid: 185431. Strain: treu927. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: codonplus ril.

Resolution:

2.10Å R-factor: 0.171 R-free: 0.230

Authors:

M.S.Alphey,S.Patterson,A.H.Fairlamb

Key ref:

S.Patterson et al. (2011). Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: discovery, synthesis, and characterization of their binding mode by protein crystallography. J Med Chem, 54, 6514-6530. PubMed id: 21851087

Date:

06-Aug-09 Release date: 13-Oct-10

Protein chains

Q389T8  (Q389T8_TRYB2) -  Trypanothione reductase from Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

Seq: 492 a.a.

Struc: 490 a.a.

Enzyme reactions

• Enzyme class: E.C.1.8.1.12 - trypanothione-disulfide reductase.
• Reaction: trypanothione + NADP⁺ = trypanothione disulfide + NADPH + H⁺
• Cofactor: FAD

FAD (Bound ligand (Het Group name = FAD) corresponds exactly)

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

reference

J Med Chem 54:6514-6530 (2011)

PubMed id: 21851087

Dihydroquinazolines as a novel class of Trypanosoma brucei trypanothione reductase inhibitors: discovery, synthesis, and characterization of their binding mode by protein crystallography.

S.Patterson, M.S.Alphey, D.C.Jones, E.J.Shanks, I.P.Street, J.A.Frearson, P.G.Wyatt, I.H.Gilbert, A.H.Fairlamb.

ABSTRACT

No abstract given.