PDBe 1idt

X-ray diffraction
2Å resolution

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

Released:

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:

Structure analysis Details

Assembly composition:
homo dimer (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

2 bound ligands:

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