PDBsum entry: 2dmr

Reductase

PDB id: 2dmr

Contents

Protein chain

771 a.a. *

Ligands

PGD ×2

__O

SO2

Metals

4MO

Waters ×107

* Residue conservation analysis

PDB id:

2dmr

Name:

Reductase

Title:

Dithionite reduced dmso reductase from rhodobacter capsulatus

Structure:

Dmso reductase. Chain: a

Source:

Rhodobacter capsulatus. Organism_taxid: 1061. Strain: h123. Cellular_location: periplasm

Resolution:

2.80Å R-factor: 0.181 R-free: 0.263

Authors:

A.S.Mcalpine,S.Bailey

Key ref:

A.S.Mcalpine et al. (1997). Molybdenum active centre of dmso reductase from rhodobacter capsulatus: crystal structure of the oxidised enzyme at 1.82-A resolution and the dithionite-Reduced enzyme at 2.8-A resolution. J biol inorg chem, 2, PubMed id: -1

Date:

24-Apr-97 Release date: 18-Mar-98

Protein chain

Q52675  (DMSA_RHOCA) -  Dimethyl sulfoxide/trimethylamine N-oxide reductase

Seq: 823 a.a.

Struc: 772 a.a.*

* PDB and UniProt seqs differ at 14 residue positions (black crosses)

Enzyme reactions

• Enzyme class 1: E.C.1.7.2.3 - Trimethylamine-N-oxide reductase (cytochrome c).
• Reaction: Trimethylamine + 2 (ferricytochrome c)-subunit + H₂O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H⁺
• Cofactor: Bis(molybdopterin guanine dinucleotide)molybdenum cofactor
• Enzyme class 2: E.C.1.8.5.3 - Dimethylsulfoxide reductase.
• Reaction: Dimethylsulfide + menaquinone + H₂O = dimethylsulfoxide + menaquinol
• Cofactor: Iron-sulfur; Molybdopterin

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

 Gene Ontology (GO) functional annotation 

• Biological process: oxidation-reduction process (1 term)
• Biochemical function: binding (5 terms)