1OCX
E. coli maltose-O-acetyltransferase
Summary for 1OCX
Entry DOI | 10.2210/pdb1ocx/pdb |
Descriptor | MALTOSE O-ACETYLTRANSFERASE, TRIMETHYL LEAD ION (3 entities in total) |
Functional Keywords | transferase, acetyl transferase, left-handed parallel beta-helix |
Biological source | ESCHERICHIA COLI |
Total number of polymer chains | 3 |
Total formula weight | 61224.83 |
Authors | Lo Leggio, L.,Dal Degan, F.,Poulsen, P.,Larsen, S. (deposition date: 2003-02-11, release date: 2003-06-12, Last modification date: 2024-05-08) |
Primary citation | Lo Leggio, L.,Degan, F.D.,Poulsen, P.,Andersen, S.M.,Larsen, S. The Structure and Specificity of Escherichia Coli Maltose Acetyltransferase Give New Insight Into the Laca Family of Acyltransferases. Biochemistry, 42:5225-, 2003 Cited by PubMed: 12731863DOI: 10.1021/BI0271446 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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