› 3h31

X-ray diffraction
1Å resolution

Structure of Rhodothermus marinus HiPIP at 1.0 A resolution

Released:
DOI: 10.2210/pdb3h31/pdb
PDB entry 3h31 coloured by chain, front view.
PDB entry 3h31 coloured by chain, side view.
PDB entry 3h31 coloured by chain, top view.
Source organism: Rhodothermus marinus
Primary publication:
Structure at 1.0 A resolution of a high-potential iron-sulfur protein involved in the aerobic respiratory chain of Rhodothermus marinus.
Stelter M, Melo AM, Hreggvidsson S, Saraiva LM, Teixeira M, Archer M
J Biol Inorg Chem 15 303-13 (2010)
PMID: 20225399

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111368 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
High potential iron-sulfur proteins family profile domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 74 amino acids
Theoretical weight: 8.1 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli
UniProt:
  • Canonical: C4P582 (Residues: 54-127; Coverage: 58%)
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 1 x SF4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA, ENRAF-NONIUS FR571
Spacegroup: P212121
Unit cell:
a: 27.267Å b: 43.343Å c: 46.787Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.104 0.104 0.144
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Structural basis for energy transduction by respiratory alternative complex III.
Sousa et al. (2018)
4 more

3 mentions without citation

Mammalian iron sulfur cluster biogenesis: From assembly to delivery to recipient proteins with a focus on novel targets of the chaperone and co-chaperone proteins.
Maio et al. (2022)
2 more