› 2zpu

X-ray diffraction
1.7Å resolution

Crystal Structure of Modified Serine Racemase from S.pombe.

Released:
DOI: 10.2210/pdb2zpu/pdb
PDB entry 2zpu coloured by chain, front view.
PDB entry 2zpu coloured by chain, side view.
PDB entry 2zpu coloured by chain, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
Serine racemase with catalytically active lysinoalanyl residue.
Yamauchi T, Goto M, Wu HY, Uo T, Yoshimura T, Mihara H, Kurihara T, Miyahara I, Hirotsu K, Esaki N
J Biochem 145 421-4 (2009)
PMID: 19155267

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129887 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: O59791 (Residues: 1-323; Coverage: 100%)
Gene names: SPCC320.14, SPCC330.15c, sry1
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand PDD 1 x PDD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 59.74Å b: 72.99Å c: 65.07Å
α: 90° β: 102.41° γ: 90°
R-values:
R R work R free
0.183 0.183 0.209
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Nutritional and medicinal aspects of D-amino acids.
Friedman et al. (2012)
1 more

4 mentions without citation

The Energy Landscape of Human Serine Racemase.
Raboni et al. (2018)
3 more