› 1a0g

X-ray diffraction
2Å resolution

L201A MUTANT OF D-AMINO ACID AMINOTRANSFERASE COMPLEXED WITH PYRIDOXAMINE-5'-PHOSPHATE

Released:
DOI: 10.2210/pdb1a0g/pdb
PDB entry 1a0g coloured by chain, front view.
PDB entry 1a0g coloured by chain, side view.
PDB entry 1a0g coloured by chain, top view.
Source organism: Bacillus sp. YM-1
Primary publication:
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko GA, Ringe D, Yoshimura T, Esaki N
Protein Eng 11 613-9 (1998)
PMID: 9749913

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: 282 amino acids
Theoretical weight: 32.27 KDa
Source organism: Bacillus sp. YM-1
Expression system: Escherichia coli
UniProt:
  • Canonical: P19938 (Residues: 2-283; Coverage: 100%)
Gene name: dat
Sequence domains: Amino-transferase class IV
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 2 x PMP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 77.34Å b: 91.76Å c: 88.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.263
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
6 other articles

1 mention without citation

Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus.
Łyskowski et al. (2014)