X-ray diffraction
2.2Å resolution

Crystal Structure of Modified Serine Racemase complexed with Serine


Function and Biology Details

Reactions catalysed:
L-serine = D-serine
(1a) D-serine = 2-aminoprop-2-enoate + H(2)O
(1a) L-serine = 2-aminoprop-2-enoate + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Serine racemase Chain: A
Molecule details ›
Chain: A
Length: 323 amino acids
Theoretical weight: 35.09 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli
  • Canonical: O59791 (Residues: 1-323; Coverage: 100%)
Gene names: SPCC320.14, SPCC330.15c, SRR
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: C2
Unit cell:
a: 59.54Å b: 72.88Å c: 64.81Å
α: 90° β: 101.73° γ: 90°
R R work R free
0.171 0.171 0.216
Expression system: Escherichia coli