PDBsum entry 4u72

Oxidoreductase

PDB id: 4u72

Contents

Protein chains

375 a.a.

Ligands

HEM-PIM ×2

NHE ×4

Waters ×335

PDB id:

4u72

Name:

Oxidoreductase

Title:

Crystal structure of 4-phenylimidazole bound form of human indoleamine 2,3-dioxygenase (a260g mutant)

Structure:

Indoleamine 2,3-dioxygenase 1. Chain: a, b. Fragment: indoleamine 2,3-dioxygenase. Synonym: ido-1,indoleamine-pyrrole 2,3-dioxygenase. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ido1, ido, indo. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.188 R-free: 0.231

Authors:

H.Sugimoto,M.Horitani,E.Kometani,Y.Shiro

Key ref:

M.Horitani et al. Conformation and mobility of active site loop is crit for substrate binding and inhibition in human indolea 2,3-Dioxygenase. To be published, .

Date:

30-Jul-14 Release date: 02-Sep-15

Protein chains

P14902  (I23O1_HUMAN) -  Indoleamine 2,3-dioxygenase 1 from Homo sapiens

Seq: 403 a.a.

Struc: 375 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.1.13.11.52 - indoleamine 2,3-dioxygenase.
• Reaction:
  1. D-tryptophan + O2 = N-formyl-D-kynurenine
  2. L-tryptophan + O2 = N-formyl-L-kynurenine

D-tryptophan (Bound ligand (Het Group name = PIM) matches with 62.50% similarity) + O2 = N-formyl-D-kynurenine

L-tryptophan (Bound ligand (Het Group name = PIM) matches with 62.50% similarity) + O2 = N-formyl-L-kynurenine

• Cofactor: Heme

Heme (Bound ligand (Het Group name = HEM) matches with 95.45% similarity)

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