› 8e9o

X-ray diffraction
1.96Å resolution

Crystal structure of E. coli aspartate aminotransferase mutant VFIY bound to maleic acid at 278 K

Released:
DOI: 10.2210/pdb8e9o/pdb
Model geometry
Fit model/data
PDB entry 8e9o coloured by chain, front view.
PDB entry 8e9o coloured by chain, side view.
PDB entry 8e9o coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Computational remodeling of an enzyme conformational landscape for altered substrate selectivity.
St-Jacques AD, Rodriguez JM, Eason MG, Foster SM, Khan ST, Damry AM, Goto NK, Thompson MC, Chica RA
OpenAccess logo Nat Commun 14 6058 (2023)
PMID: 37770431

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 406 amino acids
Theoretical weight: 44.86 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00509 (Residues: 2-396; Coverage: 100%)
Gene names: JW0911, aspC, b0928
Sequence domains: Aminotransferase class I and II

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand MAE 2 x MAE
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALS BEAMLINE 8.3.1
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
0.152 0.148 0.189
Expression system: Escherichia coli

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