› 1szk

X-ray diffraction
2.52Å resolution

The structure of gamma-aminobutyrate aminotransferase mutant: E211S

Released:
DOI: 10.2210/pdb1szk/pdb
PDB entry 1szk coloured by chain, front view.
PDB entry 1szk coloured by chain, side view.
PDB entry 1szk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase.
Liu W, Peterson PE, Langston JA, Jin X, Zhou X, Fisher AJ, Toney MD
Biochemistry 44 2982-92 (2005)
PMID: 15723541

Function and Biology Details

Reactions catalysed: 
4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate
5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-aminobutyrate aminotransferase GabT Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 426 amino acids
Theoretical weight: 45.79 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P22256 (Residues: 1-426; Coverage: 100%)
Gene names: JW2637, b2662, gabT
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PMP 4 x PMP
2 bound ligands:
Ligand SO4 15 x SO4
Ligand EDO 13 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P3221
Unit cell:
a: 108.26Å b: 108.26Å c: 300.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.187 0.24
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg et al. (2015)
3 more