› 1pwe

X-ray diffraction
2.8Å resolution

Rat Liver L-Serine Dehydratase Apo Enzyme

Released:
DOI: 10.2210/pdb1pwe/pdb
PDB entry 1pwe coloured by chain, front view.
PDB entry 1pwe coloured by chain, side view.
PDB entry 1pwe coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structure of serine dehydratase from rat liver.
Yamada T, Komoto J, Takata Y, Ogawa H, Pitot HC, Takusagawa F
Biochemistry 42 12854-65 (2003)
PMID: 14596599

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-140618 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine dehydratase/L-threonine deaminase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 327 amino acids
Theoretical weight: 34.51 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P09367 (Residues: 1-363; Coverage: 90%)
  • Best match: P09367-2 (Residues: 1-327)
Gene name: Sds
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 70.628Å b: 169.843Å c: 95.998Å
α: 90° β: 92.75° γ: 90°
R-values:
R R work R free
0.218 0.218 0.247
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
5 more

5 mentions without citation

The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.
Smith et al. (2010)
4 more