› 1icv

X-ray diffraction
2.4Å resolution

THE STRUCTURE OF ESCHERICHIA COLI NITROREDUCTASE COMPLEXED WITH NICOTINIC ACID

Released:
DOI: 10.2210/pdb1icv/pdb
PDB entry 1icv coloured by chain, front view.
PDB entry 1icv coloured by chain, side view.
PDB entry 1icv coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution.
Lovering AL, Hyde EI, Searle PF, White SA
J Mol Biol 309 203-13 (2001)
PMID: 11491290

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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 217 amino acids
Theoretical weight: 24.17 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
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 4 x FMN
1 bound ligand:
Ligand NIO 4 x NIO
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 57.74Å b: 119.57Å c: 143.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.242
Expression system: Escherichia coli BL21

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Citations

4 review citations

Biological degradation of 2,4,6-trinitrotoluene.
Esteve-Núñez et al. (2001)
3 more