› 1ye8

X-ray diffraction
1.4Å resolution

Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus

Released:
DOI: 10.2210/pdb1ye8/pdb
PDB entry 1ye8 coloured by chain, front view.
PDB entry 1ye8 coloured by chain, side view.
PDB entry 1ye8 coloured by chain, top view.
Source organism: Aquifex aeolicus
Primary publication:
Crystal structure of THEP1 from the hyperthermophile Aquifex aeolicus: a variation of the RecA fold.
Rossbach M, Daumke O, Klinger C, Wittinghofer A, Kaufmann M
BMC Struct Biol 5 7 (2005)
PMID: 15777481

Function and Biology Details

Reaction catalysed: 
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130483 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleoside-triphosphatase THEP1 Chain: A
Molecule details ›
Chain: A
Length: 178 amino acids
Theoretical weight: 20.73 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67322 (Residues: 1-178; Coverage: 100%)
Gene name: aq_1292
Sequence domains: NTPase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand NA 2 x NA
Ligand PO4 1 x PO4
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 35.87Å b: 64.24Å c: 39.62Å
α: 90° β: 105.23° γ: 90°
R-values:
R R work R free
0.174 0.172 0.207
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

NMR structure and functional characterization of a human cancer-related nucleoside triphosphatase.
Placzek et al. (2007)
1 more

2 mentions without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)
1 more