› 5j6c

X-ray diffraction
2.1Å resolution

FMN-dependent Nitroreductase (CDR20291_0767) from Clostridium difficile R20291

Released:
DOI: 10.2210/pdb5j6c/pdb
PDB entry 5j6c coloured by chain, front view.
PDB entry 5j6c coloured by chain, side view.
PDB entry 5j6c coloured by chain, top view.
Source organism: Clostridioides difficile R20291
Primary publication:
Crystal structures of two nitroreductases from hypervirulent Clostridium difficile and functionally related interactions with the antibiotic metronidazole.
Wang B, Powell SM, Hessami N, Najar FZ, Thomas LM, Karr EA, West AH, Richter-Addo GB
Nitric Oxide 60 32-39 (2016)
PMID: 27623089

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165849 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 201 amino acids
Theoretical weight: 23.3 KDa
Source organism: Clostridioides difficile R20291
Expression system: Escherichia coli BL21(DE3)
Structure domains: NADH Oxidase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 67.908Å b: 70.732Å c: 87.882Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.186 0.241
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Metronidazole: an update on metabolism, structure-cytotoxicity and resistance mechanisms.
Dingsdag et al. (2018)
2 other articles

1 mention without citation

Crystal structures of two nitroreductases from hypervirulent Clostridium difficile and functionally related interactions with the antibiotic metronidazole.
Wang et al. (2016)