1ye8

X-ray diffraction
1.4Å resolution

Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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:
1 modified residue:

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