3vvl

X-ray diffraction
1.81Å resolution

Crystal structure of L-serine-O-acetyltransferase found in D-cycloserine biosynthetic pathway

Released:

Function and Biology Details

Reactions catalysed:
Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine
Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine/homoserine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 42.49 KDa
Source organism: Streptomyces lavendulae subsp. lavendulae
Expression system: Escherichia coli
UniProt:
  • Canonical: D2Z028 (Residues: 1-374; Coverage: 100%)
Gene names: dcsE, metX
Sequence domains: alpha/beta hydrolase fold
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 46.71Å b: 102.58Å c: 146.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli