› 1idt

X-ray diffraction
2Å resolution

STRUCTURAL STUDIES ON A PRODRUG-ACTIVATING SYSTEM-CB1954 AND FMN-DEPENDENT NITROREDUCTASE

Released:
DOI: 10.2210/pdb1idt/pdb
PDB entry 1idt coloured by chain, front view.
PDB entry 1idt coloured by chain, side view.
PDB entry 1idt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form.
Johansson E, Parkinson GN, Denny WA, Neidle S
J Med Chem 46 4009-20 (2003)
PMID: 12954054

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
Expression system: Escherichia coli B
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
1 bound ligand:
Ligand CB1 2 x CB1
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P41212
Unit cell:
a: 57.556Å b: 57.556Å c: 266.129Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.225 0.268
Expression system: Escherichia coli B

Quick links

Citations

5 review citations

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