› 3wqg

X-ray diffraction
1.55Å resolution

D-threo-3-hydroxyaspartate dehydratase C353A mutant in the metal-free form

Released:
DOI: 10.2210/pdb3wqg/pdb
PDB entry 3wqg coloured by chain, front view.
PDB entry 3wqg coloured by chain, side view.
PDB entry 3wqg coloured by chain, top view.
Source organism: Delftia sp. HT23
Primary publication:
Structural insights into the substrate stereospecificity of D-threo-3-hydroxyaspartate dehydratase from Delftia sp. HT23: a useful enzyme for the synthesis of optically pure L-threo- and D-erythro-3-hydroxyaspartate.
Matsumoto Y, Yasutake Y, Takeda Y, Tamura T, Yokota A, Wada M
Appl Microbiol Biotechnol 99 7137-50 (2015)
PMID: 25715785

Function and Biology Details

Reaction catalysed: 
Threo-3-hydroxy-D-aspartate = oxaloacetate + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109505 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-threo-3-hydroxyaspartate dehydratase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 41.52 KDa
Source organism: Delftia sp. HT23
Expression system: Rhodococcus erythropolis
UniProt:
  • Canonical: B2DFG5 (Residues: 1-380; Coverage: 100%)
Gene name: dthadh
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: I4122
Unit cell:
a: 158.041Å b: 158.041Å c: 159.154Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.179
Expression system: Rhodococcus erythropolis

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Citations

3 citation in other articles

Urinary l-erythro-β-hydroxyasparagine-a novel serine racemase inhibitor and substrate of the Zn2+-dependent d-serine dehydratase.
Ito et al. (2021)
2 more