› 4f5m

X-ray diffraction
1.65Å resolution

Wild-Type E. coli Aspartate Aminotransferase: A Template For The Interconversion of Substrate Specificity and Activity To Tyrosine Aminotransferase By The JANUS Algorithm.

Released:
DOI: 10.2210/pdb4f5m/pdb
PDB entry 4f5m coloured by chain, front view.
PDB entry 4f5m coloured by chain, side view.
PDB entry 4f5m coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Janus: prediction and ranking of mutations required for functional interconversion of enzymes.
Addington TA, Mertz RW, Siegel JB, Thompson JM, Fisher AJ, Filkov V, Fleischman NM, Suen AA, Zhang C, Toney MD
J Mol Biol 425 1378-89 (2013)
PMID: 23396064

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: 45 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00509 (Residues: 2-396; Coverage: 100%)
Gene names: JW0911, aspC, b0928
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand EDO 4 x EDO
1 modified residue:
Ligand LLP 2 x LLP

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P212121
Unit cell:
a: 58.299Å b: 108.938Å c: 144.234Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.176 0.21
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.
Currin et al. (2015)
3 more

2 mentions without citation

Janus: prediction and ranking of mutations required for functional interconversion of enzymes.
Addington et al. (2013)
1 more