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Ligands
Code Name Style Show Link
0A0 2-methyl-L-aspartic acid
PLP Pyridoxal-5'-phosphate
Non-standard Residues
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Glycosylation
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Code : 1ART   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE(AMINOTRANSFERASE)
Title : X-RAY CRYSTALLOGRAPHIC STUDY OF PYRIDOXAL 5'-PHOSPHATE-TYPE ASPARTATE AMINOTRANSFERASES FROM ESCHERICHIA COLI IN OPEN AND CLOSED FORM
Release Data : 1994-08-31
Compound :
mol_id molecule chains
1 ASPARTATE AMINOTRANSFERASE A
ec: 2.6.1.1
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
Authors : Okamoto, A., Higuchi, T., Hirotsu, K.
Keywords : TRANSFERASE(AMINOTRANSFERASE)
Exp. method : X-RAY DIFFRACTION ( 1.8 Å )
Citation :

X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form.

Okamoto, A.,Higuchi, T.,Hirotsu, K.  et al.
(1994)  J.Biochem.(Tokyo)  116 : 95 - 107

PubMed: 7798192

Three-Dimensional Structure of Aspartate Aminotransferase from Escherichia Coli

Okamoto, A.,Hirotsu, K.,Higuchi, T.  et al.
(1991)  Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds as Cofactors: Proceedings of the 8Th International Symposium on Vitamin B6 and Carbonyl Catalysis  : 107

Chain : A
UniProt : P00509 (AAT_ECOLI)
Reaction: EC: Evidence:
Physiological Direction:
2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate 2.6.1.1 PubMed:10556573
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