› 1ams

X-ray diffraction
2.7Å resolution

X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAMINE 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN THREE FORMS

Released:
DOI: 10.2210/pdb1ams/pdb
PDB entry 1ams coloured by chain, front view.
PDB entry 1ams coloured by chain, side view.
PDB entry 1ams coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms.
Miyahara I, Hirotsu K, Hayashi H, Kagamiyama H
J Biochem 116 1001-12 (1994)
PMID: 7896726

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: 43.62 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


Cofactor: Ligand PMP 1 x PMP
1 bound ligand:
Ligand GUA 1 x GUA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 155.1Å b: 86.6Å c: 79.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.243 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structure, expression, and function of kynurenine aminotransferases in human and rodent brains.
Han et al. (2010)
1 more

1 mention without citation

Discriminative structural approaches for enzyme active-site prediction.
Kato et al. (2011)