› 4am2

X-ray diffraction
1.8Å resolution

Bacterioferritin from Blastochloris viridis

Released:
DOI: 10.2210/pdb4am2/pdb
PDB entry 4am2 coloured by chain, front view.
PDB entry 4am2 coloured by chain, side view.
PDB entry 4am2 coloured by chain, top view.
Source organism: Blastochloris viridis
Primary publication:
Structural characterization of bacterioferritin from Blastochloris viridis.
Wahlgren WY, Omran H, von Stetten D, Royant A, van der Post S, Katona G
PLoS One 7 e46992 (2012)
PMID: 23056552

Function and Biology Details

Reaction catalysed: 
4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125593 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bacterioferritin Chains: A, B
Molecule details ›
Chains: A, B
Length: 159 amino acids
Theoretical weight: 18.39 KDa
Source organism: Blastochloris viridis
UniProt:
  • Canonical: K7N5M0 (Residues: 1-159; Coverage: 100%)
Gene names: BV133_1877, BVIRIDIS_22540, bfr
Sequence domains: Ferritin-like domain
Structure domains: Ferritin

Ligands and Environments

2 bound ligands:
Ligand HEM 1 x HEM
Ligand FE 4 x FE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: F23
Unit cell:
a: 170.2Å b: 170.2Å c: 170.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.155 0.192

Quick links

Citations

4 citation in other articles

Deciphering the GPER/GPR30-agonist and antagonists interactions using molecular modeling studies, molecular dynamics, and docking simulations.
Méndez-Luna et al. (2015)
3 more

4 mentions without citation

Hepatitis C virus RNA replication depends on specific cis- and trans-acting activities of viral nonstructural proteins.
Kazakov et al. (2015)
3 more