› 3hip

X-ray diffraction
2.8Å resolution

HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM PURPURATUM

Released:
DOI: 10.2210/pdb3hip/pdb
PDB entry 3hip coloured by chain, front view.
PDB entry 3hip coloured by chain, side view.
PDB entry 3hip coloured by chain, top view.
Source organism: Marichromatium purpuratum
Primary publication:
Crystal structure and possible dimerization of the high-potential iron-sulfur protein from Chromatium purpuratum.
Kerfeld CA, Salmeen AE, Yeates TO
Biochemistry 37 13911-7 (1998)
PMID: 9760225

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157930 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High-potential iron-sulfur protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 82 amino acids
Theoretical weight: 8.76 KDa
Source organism: Marichromatium purpuratum
UniProt:
  • Canonical: P59860 (Residues: 1-82; Coverage: 100%)
Gene name: hip
Sequence domains: High potential iron-sulfur protein
Structure domains: High potential iron-sulphur protein

Ligands and Environments

1 bound ligand:
Ligand SF4 3 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21212
Unit cell:
a: 55.5Å b: 108.8Å c: 37.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.288

Quick links

Citations

1 review citation

Structural and functional studies on the tetraheme cytochrome subunit and its electron donor proteins: the possible docking mechanisms during the electron transfer reaction.
Nogi et al. (2005)
13 other articles

1 mention without citation

Arginine and Lysine interactions with π residues in metalloproteins.
Anitha et al. (2012)