› 2zy4

X-ray diffraction
2Å resolution

dodecameric L-aspartate beta-decarboxylase

Released:
DOI: 10.2210/pdb2zy4/pdb
PDB entry 2zy4 coloured by chain, front view.
PDB entry 2zy4 coloured by chain, side view.
PDB entry 2zy4 coloured by chain, top view.
Source organism: Alcaligenes faecalis subsp. faecalis
Primary publication:
Structure, assembly, and mechanism of a PLP-dependent dodecameric L-aspartate beta-decarboxylase.
Chen HJ, Ko TP, Lee CY, Wang NC, Wang AH
Structure 17 517-29 (2009)
PMID: 19368885

Function and Biology Details

Reactions catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
L-aspartate = L-alanine + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188117 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 546 amino acids
Theoretical weight: 61.17 KDa
Source organism: Alcaligenes faecalis subsp. faecalis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93QX0 (Residues: 1-533; Coverage: 100%)
Gene name: asD
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 6 x PLP
1 bound ligand:
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: C2221
Unit cell:
a: 149.953Å b: 217.149Å c: 207.154Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.204
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe.
Jeong et al. (2019)