2zau

X-ray diffraction
2Å resolution

Crystal structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus

Released:
Source organism: Aquifex aeolicus
Primary publication:
Structure of an N-terminally truncated selenophosphate synthetase from Aquifex aeolicus.
Acta Crystallogr Sect F Struct Biol Cryst Commun 64 453-8 (2008)
PMID: 18540050

Function and Biology Details

Reaction catalysed:
ATP + selenide + H(2)O = AMP + selenophosphate + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
PDBe Complex ID:
PDB-CPX-130450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Selenide, water dikinase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 311 amino acids
Theoretical weight: 34.26 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67139 (Residues: 26-336; Coverage: 93%)
Gene names: aq_1030, selD
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2221
Unit cell:
a: 93.161Å b: 165.198Å c: 167.684Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.239
Expression system: Escherichia coli