› 2fcr

X-ray diffraction
1.8Å resolution

CRYSTAL STRUCTURE OF OXIDIZED FLAVODOXIN FROM A RED ALGA CHONDRUS CRISPUS REFINED AT 1.8 ANGSTROMS RESOLUTION: DESCRIPTION OF THE FLAVIN MONONUCLEOTIDE BINDING SITE

Released:
DOI: 10.2210/pdb2fcr/pdb
PDB entry 2fcr coloured by chain, front view.
PDB entry 2fcr coloured by chain, side view.
PDB entry 2fcr coloured by chain, top view.
Source organism: Chondrus crispus
Primary publication:
Crystal structure of oxidized flavodoxin from a red alga Chondrus crispus refined at 1.8 A resolution. Description of the flavin mononucleotide binding site.
Fukuyama K, Matsubara H, Rogers LJ
J Mol Biol 225 775-89 (1992)
PMID: 1602481

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-146844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavodoxin Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 18.89 KDa
Source organism: Chondrus crispus
Expression system: Not provided
UniProt:
  • Canonical: P14070 (Residues: 1-173; 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: P212121
Unit cell:
a: 63.57Å b: 48.83Å c: 56.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 not available not available
Expression system: Not provided

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Citations

1 review citation

Characteristics of the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans as revealed by biochemical, biophysical, and molecular biological approaches.
Yagi et al. (1993)
24 other articles

9 mentions without citation

The shadow map: a general contact definition for capturing the dynamics of biomolecular folding and function.
Noel et al. (2012)
8 more