› 4cvq

X-ray diffraction
2.11Å resolution

CRYSTAL STRUCTURE OF AN AMINOTRANSFERASE FROM ESCHERICHIA COLI AT 2. 11 ANGSTROEM RESOLUTION

Released:
DOI: 10.2210/pdb4cvq/pdb
PDB entry 4cvq coloured by chain, front view.
PDB entry 4cvq coloured by chain, side view.
PDB entry 4cvq coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.
Peña-Soler E, Fernandez FJ, López-Estepa M, Garces F, Richardson AJ, Quintana JF, Rudd KE, Coll M, Vega MC
OpenAccess logo PLoS One 9 e102139 (2014)
PMID: 25014014

Function and Biology Details

Reaction catalysed: 
L-alanine + 2-oxoglutarate = pyruvate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate-pyruvate aminotransferase AlaA Chains: A, B
Molecule details ›
Chains: A, B
Length: 431 amino acids
Theoretical weight: 48.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A959 (Residues: 1-405; Coverage: 100%)
Gene names: JW2287, alaA, b2290, yfbQ
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
2 bound ligands:
Ligand ACT 2 x ACT
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 59.78Å b: 152.13Å c: 174.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

RidA Proteins Protect against Metabolic Damage by Reactive Intermediates.
Irons et al. (2020)
1 more

1 mention without citation

Structural analysis and mutant growth properties reveal distinctive enzymatic and cellular roles for the three major L-alanine transaminases of Escherichia coli.
Peña-Soler et al. (2014)