› 1x28

X-ray diffraction
2.4Å resolution

Crystal Structure of e.coli AspAT complexed with N-phosphopyridoxyl-L-glutamic acid

Released:
DOI: 10.2210/pdb1x28/pdb
PDB entry 1x28 coloured by chain, front view.
PDB entry 1x28 coloured by chain, side view.
PDB entry 1x28 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Binding of C5-dicarboxylic substrate to aspartate aminotransferase: implications for the conformational change at the transaldimination step.
Islam MM, Goto M, Miyahara I, Ikushiro H, Hirotsu K, Hayashi H
Biochemistry 44 8218-29 (2005)
PMID: 15938611

Function and Biology Details

Reaction catalysed: 
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

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 Chains: A, B
Molecule details ›
Chains: A, B
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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P63
Unit cell:
a: 143.83Å b: 143.83Å c: 81.57Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.243
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Direct evidence for a glutamate switch necessary for substrate recognition: crystal structures of lysine epsilon-aminotransferase (Rv3290c) from Mycobacterium tuberculosis H37Rv.
Mani Tripathi et al. (2006)
7 more

3 mentions without citation

Structural Insights into a Novel Class of Aspartate Aminotransferase from Corynebacterium glutamicum.
Son et al. (2016)
2 more