› 4h27

X-ray diffraction
1.3Å resolution

Modulating the function of human serine racemase and human serine dehydratase by protein engineering

Released:
DOI: 10.2210/pdb4h27/pdb
PDB entry 4h27 coloured by chain, front view.
PDB entry 4h27 coloured by chain, side view.
PDB entry 4h27 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Modulating the function of human serine racemase and human serine dehydratase by protein engineering.
Wang CY, Ku SC, Lee CC, Wang AH
Protein Eng Des Sel 25 741-9 (2012)
PMID: 23112234

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine dehydratase/L-threonine deaminase Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 38.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P20132 (Residues: 1-328; Coverage: 100%)
Gene names: SDH, SDS
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand LLP 1 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: I422
Unit cell:
a: 158.502Å b: 158.502Å c: 59.453Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.144 0.168
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position 84 as a hot spot for β-elimination function.
Nelson et al. (2017)
3 more

3 mentions without citation

Human Serine Racemase: Key Residues/Active Site Motifs and Their Relation to Enzyme Function.
Graham et al. (2019)
2 more