› 1isu

X-ray diffraction
1.5Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF THE HIGH-POTENTIAL IRON-SULFUR PROTEIN ISOLATED FROM THE PURPLE PHOTOTROPHIC BACTERIUM RHODOCYCLUS TENUIS DETERMINED AND REFINED AT 1.5 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1isu/pdb
PDB entry 1isu coloured by chain, front view.
PDB entry 1isu coloured by chain, side view.
PDB entry 1isu coloured by chain, top view.
Source organism: Rhodocyclus tenuis
Primary publication:
Three-dimensional structure of the high-potential iron-sulfur protein isolated from the purple phototrophic bacterium Rhodocyclus tenuis determined and refined at 1.5 A resolution.
Rayment I, Wesenberg G, Meyer TE, Cusanovich MA, Holden HM
J Mol Biol 228 672-86 (1992)
PMID: 1453470

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152636 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High-potential iron-sulfur protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 62 amino acids
Theoretical weight: 6.3 KDa
Source organism: Rhodocyclus tenuis
Expression system: Not provided
UniProt:
  • Canonical: P33678 (Residues: 1-62; 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 2 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 36.7Å b: 52.6Å c: 27.6Å
α: 90° β: 90.8° γ: 90°
R-values:
R R work R free
0.173 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
3 more

15 mentions without citation

Peptide-plane flipping in proteins.
Hayward S. (2001)
14 more