› 1doi

X-ray diffraction
1.9Å resolution

2FE-2S FERREDOXIN FROM HALOARCULA MARISMORTUI

Released:
DOI: 10.2210/pdb1doi/pdb
PDB entry 1doi coloured by chain, front view.
PDB entry 1doi coloured by chain, side view.
PDB entry 1doi coloured by chain, top view.
Source organism: Haloarcula marismortui
Primary publication:
Insights into protein adaptation to a saturated salt environment from the crystal structure of a halophilic 2Fe-2S ferredoxin.
Frolow F, Harel M, Sussman JL, Mevarech M, Shoham M
Nat Struct Biol 3 452-8 (1996)
PMID: 8612076

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132330 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ferredoxin-1 Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 14.41 KDa
Source organism: Haloarcula marismortui
UniProt:
  • Canonical: P00217 (Residues: 2-129; Coverage: 99%)
Gene names: fer1, rrnAC2526
Sequence domains: 2Fe-2S iron-sulfur cluster binding domain
Structure domains: Ubiquitin-like (UB roll)

Ligands and Environments

2 bound ligands:
Ligand K 6 x K
Ligand FES 1 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P6322
Unit cell:
a: 59.18Å b: 59.18Å c: 124.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 not available

Quick links

Citations

17 review citations

The stability of proteins in extreme environments.
Jaenicke et al. (1998)
16 more

11 mentions without citation

Physics and evolution of thermophilic adaptation.
Berezovsky et al. (2005)
10 more