3d64

X-ray diffraction
2.3Å resolution

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Burkholderia pseudomallei

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylhomocysteinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 494 amino acids
Theoretical weight: 54.56 KDa
Source organism: Burkholderia pseudomallei 1710b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3JY79 (Residues: 1-473; Coverage: 100%)
Gene names: BURPS1710b_0057, ahcY
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3221
Unit cell:
a: 186.363Å b: 186.363Å c: 104.403Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.172 0.171 0.202
Expression system: Escherichia coli