› 4f5l

X-ray diffraction
1.4Å resolution

A Theoretical Optimized Mutant for the Conversion of Substrate Specificity and Activity of Aspartate Aminotransferase to Tyrosine Aminotransferase: Chimera P7.

Released:
DOI: 10.2210/pdb4f5l/pdb
PDB entry 4f5l coloured by chain, front view.
PDB entry 4f5l coloured by chain, side view.
PDB entry 4f5l coloured by chain, top view.
Source organism: Escherichia coli K-12
Entry authors: Addington TA, Fisher AJ, Toney MD

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: 44.78 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 13 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: 59.736Å b: 102.99Å c: 139.304Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.181
Expression system: Escherichia coli BL21(DE3)

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