› 1spa

X-ray diffraction
2Å resolution

ROLE OF ASP222 IN THE CATALYTIC MECHANISM OF ESCHERICHIA COLI ASPARTATE AMINOTRANSFERASE: THE AMINO ACID RESIDUE WHICH ENHANCES THE FUNCTION OF THE ENZYME-BOUND COENZYME PYRIDOXAL 5'-PHOSPHATE

Released:
DOI: 10.2210/pdb1spa/pdb
PDB entry 1spa coloured by chain, front view.
PDB entry 1spa coloured by chain, side view.
PDB entry 1spa coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H
Biochemistry 31 5878-87 (1992)
PMID: 1610831

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 Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 43.58 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


Cofactor: Ligand NPL 1 x NPL
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 154.8Å b: 86.2Å c: 79.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

PLP-dependent H(2)S biogenesis.
Singh et al. (2011)
2 more

3 mentions without citation

Antimicrobial Peptides with Antibacterial Activity against Vancomycin-Resistant Staphylococcus aureus Strains: Classification, Structures, and Mechanisms of Action.
Hernández-Aristizábal et al. (2021)
2 more