PDBe 2v8h

X-ray diffraction
2Å resolution

Crystal structure of mutant E159A of beta-alanine synthase from Saccharomyces kluyveri in complex with its substrate N-carbamyl-beta- alanine

Released:

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
Macromolecule:
Beta-alanine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 474 amino acids
Theoretical weight: 51.95 KDa
Source organism: Lachancea kluyveri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96W94 (Residues: 2-455; Coverage: 100%)
Gene name: PYD3
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 49.78Å b: 218.3Å c: 81.58Å
α: 90° β: 92.19° γ: 90°
R-values:
R R work R free
0.18 0.178 0.208
Expression system: Escherichia coli BL21(DE3)