2yvu

X-ray diffraction
2.1Å resolution

Crystal structure of APE1195

Released:
Source organism: Aeropyrum pernix K1
Entry authors: Ishii R, Bessho Y, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable adenylyl-sulfate kinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 21.12 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YCR6 (Residues: 1-183; Coverage: 100%)
Gene names: APE_1195.1, cysC
Sequence domains: Adenylylsulphate kinase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P21
Unit cell:
a: 44.01Å b: 102.82Å c: 45.58Å
α: 90° β: 96.67° γ: 90°
R-values:
R R work R free
0.202 0.202 0.249
Expression system: Escherichia coli