› 3qpg

X-ray diffraction
1.79Å resolution

Crystal Structures of Escherichia coli Aspartate Aminotransferase Reconstituted with 1-Deaza-Pyridoxal 5'-Phosphate: Internal Aldimine and Stable L-Aspartate External Aldimine

Released:
DOI: 10.2210/pdb3qpg/pdb
PDB entry 3qpg coloured by chain, front view.
PDB entry 3qpg coloured by chain, side view.
PDB entry 3qpg coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of aspartate aminotransferase reconstituted with 1-deazapyridoxal 5'-phosphate: internal aldimine and stable L-aspartate external aldimine.
Griswold WR, Fisher AJ, Toney MD
Biochemistry 50 5918-24 (2011)
PMID: 21627105

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + 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-132575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.62 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00509 (Residues: 1-396; Coverage: 100%)
Gene names: JW0911, aspC, b0928
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand SO4 8 x SO4
Ligand EDO 4 x EDO
Ligand CL 1 x CL
Ligand 3QP 1 x 3QP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 83.785Å b: 154.834Å c: 77.799Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.148 0.179
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Aspartate aminotransferase: an old dog teaches new tricks.
Toney MD. (2014)
1 more