› 1ahn

X-ray diffraction
2.6Å resolution

E. COLI FLAVODOXIN AT 2.6 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1ahn/pdb
PDB entry 1ahn coloured by chain, front view.
PDB entry 1ahn coloured by chain, side view.
PDB entry 1ahn coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
A flavodoxin that is required for enzyme activation: the structure of oxidized flavodoxin from Escherichia coli at 1.8 A resolution.
Hoover DM, Ludwig ML
Protein Sci 6 2525-37 (1997)
PMID: 9416602

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158453 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Flavodoxin 1 Chain: A
Molecule details ›
Chain: A
Length: 175 amino acids
Theoretical weight: 19.62 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P61949 (Residues: 2-176; Coverage: 99%)
Gene names: JW0671, b0684, fldA
Sequence domains: Flavodoxin
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand FMN 1 x FMN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P312
Unit cell:
a: 78.83Å b: 78.83Å c: 52.07Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Variations on a (t)heme--novel mechanisms, redox partners and catalytic functions in the cytochrome P450 superfamily.
Munro et al. (2007)
2 more

6 mentions without citation

Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.
Houben et al. (2020)
5 more