› 3l6c

X-ray diffraction
2.2Å resolution

X-ray crystal structure of rat serine racemase in complex with malonate a potent inhibitor

Released:
DOI: 10.2210/pdb3l6c/pdb
PDB entry 3l6c coloured by chain, front view.
PDB entry 3l6c coloured by chain, side view.
PDB entry 3l6c coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J
J Biol Chem 285 12873-81 (2010)
PMID: 20106978

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-181152 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 339 amino acids
Theoretical weight: 36.58 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q76EQ0 (Residues: 1-333; Coverage: 100%)
Gene name: Srr
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
Ligand MN 2 x MN
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3
Unit cell:
a: 110.593Å b: 110.593Å c: 47.917Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.216 0.267
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Controlling reaction specificity in pyridoxal phosphate enzymes.
Toney MD. (2011)
5 more

5 mentions without citation

Current Advances on Structure-Function Relationships of Pyridoxal 5'-Phosphate-Dependent Enzymes.
Liang et al. (2019)
4 more