› 2zy2

X-ray diffraction
3.3Å resolution

dodecameric L-aspartate beta-decarboxylase

Released:
DOI: 10.2210/pdb2zy2/pdb
PDB entry 2zy2 coloured by chain, front view.
PDB entry 2zy2 coloured by chain, side view.
PDB entry 2zy2 coloured by chain, top view.
Source organism: Pseudomonas sp. ATCC 19121
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-176109 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional aspartate aminotransferase and L-aspartate beta-decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 544 amino acids
Theoretical weight: 60.84 KDa
Source organism: Pseudomonas sp. ATCC 19121
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53IZ1 (Residues: 1-531; Coverage: 100%)
Gene name: asD
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: F432
Unit cell:
a: 298.9Å b: 298.9Å c: 298.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.228 0.293
Expression system: Escherichia coli

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Citations

2 review citations

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