› 3daa

X-ray diffraction
1.9Å resolution

CRYSTALLOGRAPHIC STRUCTURE OF D-AMINO ACID AMINOTRANSFERASE INACTIVATED BY PYRIDOXYL-D-ALANINE

Released:
DOI: 10.2210/pdb3daa/pdb
PDB entry 3daa coloured by chain, front view.
PDB entry 3daa coloured by chain, side view.
PDB entry 3daa coloured by chain, top view.
Source organism: Bacillus sp. YM-1
Primary publication:
Crystallographic study of steps along the reaction pathway of D-amino acid aminotransferase.
Peisach D, Chipman DM, Van Ophem PW, Manning JM, Ringe D
Biochemistry 37 4958-67 (1998)
PMID: 9538014

Function and Biology Details

Reaction catalysed: 
D-alanine + 2-oxoglutarate = pyruvate + D-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
D-alanine aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 277 amino acids
Theoretical weight: 31.72 KDa
Source organism: Bacillus sp. YM-1
Expression system: Escherichia coli
UniProt:
  • Canonical: P19938 (Residues: 2-278; Coverage: 98%)
Gene name: dat
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PDD 2 x PDD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 77.1Å b: 78.3Å c: 88.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.245
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
9 more

7 mentions without citation

Glycoprotein composition along the pistil of Malus x domestica and the modulation of pollen tube growth.
Losada et al. (2014)
6 more