X-ray diffraction
2.8Å resolution

Crystal structure of beta-alanine synthase from Saccharomyces kluyveri (selenomethionine substituted protein)


Function and Biology Details

Reaction catalysed:
3-ureidopropanoate + H(2)O = beta-alanine + CO(2) + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
M20_dimer domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 463 amino acids
Theoretical weight: 51.28 KDa
Source organism: Lachancea kluyveri
Expression system: Escherichia coli
  • Canonical: Q96W94 (Residues: 1-455; Coverage: 100%)
Gene name: PYD3
Sequence domains: Peptidase family M20/M25/M40
Structure domains:

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 60.43Å b: 77.63Å c: 110.57Å
α: 90° β: 95.63° γ: 90°
R R work R free
0.214 0.211 0.274
Expression system: Escherichia coli