› 1ds7

X-ray diffraction
2.06Å resolution

A MINOR FMN-DEPENDENT NITROREDUCTASE FROM ESCHERICHIA COLI B

Released:
DOI: 10.2210/pdb1ds7/pdb
PDB entry 1ds7 coloured by chain, front view.
PDB entry 1ds7 coloured by chain, side view.
PDB entry 1ds7 coloured by chain, top view.
Source organism: Escherichia coli B
Primary publication:
Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme.
Parkinson GN, Skelly JV, Neidle S
J Med Chem 43 3624-31 (2000)
PMID: 11020276

Function and Biology Details

Reaction catalysed: 
A 5,6,7,8-tetrahydropteridine + NAD(P)(+) = a 6,7-dihydropteridine + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen-insensitive NAD(P)H nitroreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 217 amino acids
Theoretical weight: 23.94 KDa
Source organism: Escherichia coli B
Expression system: Escherichia coli
UniProt:
  • Canonical: P38489 (Residues: 1-217; Coverage: 100%)
Gene names: JW0567, b0578, dprA, nfnB, nfsB, nfsI, ntr
Sequence domains: Nitroreductase family
Structure domains: NADH Oxidase

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P41212
Unit cell:
a: 57.74Å b: 57.74Å c: 275.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.203 0.267
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Reduction of polynitroaromatic compounds: the bacterial nitroreductases.
Roldán et al. (2008)
9 more

7 mentions without citation

The distribution and mechanism of iodotyrosine deiodinase defied expectations.
Sun et al. (2017)
6 more