1SPA
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
Summary for 1SPA
Entry DOI | 10.2210/pdb1spa/pdb |
Descriptor | ASPARTATE AMINOTRANSFERASE, N-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE (3 entities in total) |
Functional Keywords | transferase(aminotransferase) |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P00509 |
Total number of polymer chains | 1 |
Total formula weight | 43838.41 |
Authors | Hinoue, Y.,Yano, T.,Metzler, D.E.,Miyahara, I.,Hirotsu, K.,Kagamiyama, H. (deposition date: 1993-01-26, release date: 1993-10-31, Last modification date: 2024-02-14) |
Primary citation | Yano, T.,Kuramitsu, S.,Tanase, S.,Morino, Y.,Kagamiyama, H. 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. Biochemistry, 31:5878-5887, 1992 Cited by PubMed: 1610831DOI: 10.1021/bi00140a025 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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