› 3l6r

X-ray diffraction
1.7Å resolution

The structure of mammalian serine racemase: Evidence for conformational changes upon inhibitor binding

Released:
DOI: 10.2210/pdb3l6r/pdb
PDB entry 3l6r coloured by chain, front view.
PDB entry 3l6r coloured by chain, side view.
PDB entry 3l6r coloured by chain, top view.
Source organism: Homo sapiens
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-190449 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine racemase Chain: A
Molecule details ›
Chain: A
Length: 346 amino acids
Theoretical weight: 37.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9GZT4 (Residues: 1-340; Coverage: 100%)
Gene name: SRR
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand MLI 1 x MLI
Ligand MN 1 x MN
2 modified residues:
Ligand MSE 5 x MSE
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P21212
Unit cell:
a: 54.543Å b: 84.212Å c: 70.376Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.202
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

3 mentions without citation

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