Brand  (β version)

PDB ID: 1AJS

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Ligands
Code Name Style Show Link
PLA 2-[(3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl)-amino]-2-methyl-succinic acid PoSSuM
Non-standard Residues
Code Name Show
LLP (2s)-2-amino-6-[[3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl]methylideneamino]hexanoic acid
Glycosylation
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Modification
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Structure summary

Code : 1AJS   PDBj   RCSB PDB   PDBe
Header : AMINOTRANSFERASE
Title : REFINEMENT AND COMPARISON OF THE CRYSTAL STRUCTURES OF PIG CYTOSOLIC ASPARTATE AMINOTRANSFERASE AND ITS COMPLEX WITH 2-METHYLASPARTATE
Release Data : 1997-08-20
Compound :
mol_id molecule chains
1 ASPARTATE AMINOTRANSFERASE A
ec: 2.6.1.1
other_details: THE COENZYME PYRIDOXAL 5'-PHOSPHATE IN SUBUNIT A FORMS A SCHIFF BASE WITH THE SUBSTRATE ANALOG 2-METHYLASPARTATE, AND FORMS THE EXTERNAL ALDIMINE. BUT DUE TO CRYSTAL LATTICE PACKINGS THE COENZYME IN SUBUNIT B IS STILL IN THE INTERNAL ALDIMINE WITH THE SIDE CHAIN OF LYS 258.
mol_id molecule chains
2 ASPARTATE AMINOTRANSFERASE B
ec: 2.6.1.1
other_details: THE COENZYME PYRIDOXAL 5'-PHOSPHATE IN SUBUNIT A FORMS A SCHIFF BASE WITH THE SUBSTRATE ANALOG 2-METHYLASPARTATE, AND FORMS THE EXTERNAL ALDIMINE. BUT DUE TO CRYSTAL LATTICE PACKINGS THE COENZYME IN SUBUNIT B IS STILL IN THE INTERNAL ALDIMINE WITH THE SIDE CHAIN OF LYS 258.
Source :
mol_id organism_scientific organism_common
1 Sus scrofa  (taxid:9823) Pig
mol_id organism_scientific organism_common
2 Sus scrofa  (taxid:9823) Pig
Authors : Rhee, S., Silva, M.M., Hyde, C.C., Rogers, P.H., Metzler, C.M., Metzler, D.E., Arnone, A.
Keywords : CYTOSOLIC ASPARTATE AMINOTRANSFERASE, PIG, IN THE PRESENCE OF LIGAND 2-METHYLASPARTATE, AMINOTRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 1.60 Å )
Citation :

Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate.

Rhee, S.,Silva, M.M.,Hyde, C.C.  et al.
(1997)  J.Biol.Chem.  272 : 17293 - 17302

PubMed: 9211866
DOI: 10.1074/jbc.272.28.17293

Pig Cytosolic Aspartate Aminotransferase

Arnone, A.,Rogers, P.H.,Hyde, C.C.  et al.
(1985)  Transaminases  : 138

Reaction

Chain : B
UniProt : P00503 (AATC_PIG)
Reaction: EC: Evidence:
Physiological Direction:
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate 2.6.1.1 PubMed:4634443
left-to-right UniProtKB:P13221
L-cysteine + 2-oxoglutarate = 2-oxo-3-sulfanylpropanoate + L- glutamate 2.6.1.3 PubMed:4634443
left-to-right UniProtKB:P13221
(2S)-2-aminobutanoate + 2-oxoglutarate = 2-oxobutanoate + L- glutamate - UniProtKB:P17174
right-to-left
3-sulfino-L-alanine + 2-oxoglutarate = 3-sulfinopyruvate + L- glutamate - UniProtKB:P13221
right-to-left
Cofactor: Evidence: Note:
pyridoxal 5'-phosphate ECO:0000269 | PubMed:5809231
ECO:0000269 | PubMed:9211866
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