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Ligands
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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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Code : 1BQD   PDBj   RCSB PDB   PDBe
Header : AMINOTRANSFERASE
Title : ASPARTATE AMINOTRANSFERASE P138A/P195A DOUBLE MUTANT
Release Data : 1999-05-11
Compound :
mol_id molecule chains synonym
1 ASPARTATE AMINOTRANSFERASE A,B ASPARTATE TRANSAMINASE
ec: 2.6.1.1
mutation: P138A, P195A
other_details: SCHIFF BASE BETWEEN LYS 258 AND COFACTOR, PYRIDOXAL-5'-PHOSPHATE (PLP)
Source :
mol_id organism_scientific expression_system
1 Escherichia coli  (taxid:562) Escherichia coli  (taxid:562)
strain: TY103
expression_system_plasmid: PKDHE19
Authors : Malashkevich, V.N., Jansonius, J.N.
Keywords : TRANSFERASE, AMINOTRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.1 Å )
Citation :

Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.

Birolo, L.,Malashkevich, V.N.,Capitani, G.  et al.
(1999)  Biochemistry  38 : 905 - 913

PubMed: 9893985
DOI: 10.1021/bi981467d

Chain : A, B
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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