ISDA: 3AMZ

Deposition Date 2010-08-27

Release Date 2010-12-01

Last Version Date 2026-08-12

Entry Detail

PDB ID:

3AMZ

Keywords:

OXIDOREDUCTASE

Title:

Bovine Xanthine Oxidoreductase urate bound form

Biological Source:

Source Organism(s):

Bos taurus (Taxon ID: 9913)

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

2.10 Å

R-Value Free:

0.20

R-Value Work:

0.15

R-Value Observed:

0.15

Space Group:

C 1 2 1

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Xanthine dehydrogenase/oxidas
Gene (Uniprot):XDH
Chain IDs:A, B
Chain Length:1332
Number of Molecules:2
Biological Source:Bos taurus

UniProt ID:P80457 Pfam ID:PF00111, PF01799, PF00941, PF03450, PF01315, PF02738, PF20256 EC:1.17.1.4

Ligand Molecules

BCT

FAD

FES

GOL

MOS

MTE

NAI

URC

Primary Citation

Crystal Structures of Urate Bound Form of Xanthine Oxidoreductase: Substrate Orientation and Structure of the Key Reaction Intermediate

Okamoto, K, Kawaguchi, Y, Eger, B.T, Pai, E.F, Nishino, T.Show

J.Am.Chem.Soc. 132 17080 17083 (2010)

PMID: 21077683 DOI: 10.1021/ja1077574

Abstact

Two contradictory models have been proposed for the binding mode of the substrate xanthine to and its activation mechanism by xanthine oxidoreductase. In an effort to distinguish between the two models, we determined the crystal structures of the urate complexes of the demolybdo-form of the D428A mutant of rat xanthine oxidoreductase at 1.7 Å and of the reduced bovine milk enzyme at 2.1 Å, the latter representing a reaction intermediate. The results clearly indicate the catalytically relevant binding mode of the substrate xanthine.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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