› 2fox

X-ray diffraction
1.8Å resolution

CLOSTRIDIUM BEIJERINCKII FLAVODOXIN: SEMIQUINONE

Released:
DOI: 10.2210/pdb2fox/pdb
PDB entry 2fox coloured by chain, front view.
PDB entry 2fox coloured by chain, side view.
PDB entry 2fox coloured by chain, top view.
Source organism: Clostridium beijerinckii
Primary publication:
Control of oxidation-reduction potentials in flavodoxin from Clostridium beijerinckii: the role of conformation changes.
Ludwig ML, Pattridge KA, Metzger AL, Dixon MM, Eren M, Feng Y, Swenson RP
Biochemistry 36 1259-80 (1997)
PMID: 9063874

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavodoxin Chain: A
Molecule details ›
Chain: A
Length: 138 amino acids
Theoretical weight: 15.34 KDa
Source organism: Clostridium beijerinckii
UniProt:
  • Canonical: P00322 (Residues: 1-138; Coverage: 100%)
Sequence domains: Flavodoxin
Structure domains: Rossmann fold

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3121
Unit cell:
a: 61.63Å b: 61.63Å c: 70.98Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 not available

Quick links

Citations

8 review citations

What's in a covalent bond? On the role and formation of covalently bound flavin cofactors.
Heuts et al. (2009)
7 more

9 mentions without citation

Tools for integrated sequence-structure analysis with UCSF Chimera.
Meng et al. (2006)
8 more