PDBe 3fd5

X-ray diffraction
1.9Å resolution

Crystal structure of human selenophosphate synthetase 1 complex with AMPCP

Source organism: Homo sapiens
Primary publication:
Crystal structures of catalytic intermediates of human selenophosphate synthetase 1.
J. Mol. Biol. 390 747-59 (2009)
PMID: 19477186

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Selenide, water dikinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 43.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P49903 (Residues: 1-392; Coverage: 100%)
Gene names: SELD, SEPHS1, SPS, SPS1
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P43
Unit cell:
a: 66.734Å b: 66.734Å c: 181.168Å
α: 90° β: 90° γ: 90°
R R work R free
0.14 0.138 0.195
Expression system: Escherichia coli