› 1f5v

X-ray diffraction
1.7Å resolution

STRUCTURE AND SITE-DIRECTED MUTAGENESIS OF A FLAVOPROTEIN FROM ESCHERICHIA COLI THAT REDUCES NITROCOMPOUNDS. ALTERATION OF PYRIDINE NUCLEOTIDE BINDING BY A SINGLE AMINO ACID SUBSTITUTION

Released:
DOI: 10.2210/pdb1f5v/pdb
PDB entry 1f5v coloured by chain, front view.
PDB entry 1f5v coloured by chain, side view.
PDB entry 1f5v coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and site-directed mutagenesis of a flavoprotein from Escherichia coli that reduces nitrocompounds: alteration of pyridine nucleotide binding by a single amino acid substitution.
Kobori T, Sasaki H, Lee WC, Zenno S, Saigo K, Murphy ME, Tanokura M
J Biol Chem 276 2816-23 (2001)
PMID: 11034992

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147870 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen-insensitive NADPH nitroreductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 240 amino acids
Theoretical weight: 26.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P17117 (Residues: 1-240; Coverage: 100%)
Gene names: JW0835, b0851, mda18, mdaA, nfsA, ybjB
Sequence domains: Nitroreductase family
Structure domains: NADH Oxidase

Ligands and Environments

1 bound ligand:
Ligand FMN 2 x FMN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P1
Unit cell:
a: 51.56Å b: 52.86Å c: 52.83Å
α: 75.79° β: 60.71° γ: 61.17°
R-values:
R R work R free
0.189 0.189 0.206
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Biodegradation of aromatic compounds by Escherichia coli.
Díaz et al. (2001)
7 more

16 mentions without citation

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