1EIX
STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP
Summary for 1EIX
Entry DOI | 10.2210/pdb1eix/pdb |
Descriptor | OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE, 1-(5'-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC ACID (3 entities in total) |
Functional Keywords | alpha-beta-barrel, protein-inhibitor complex, homodimer, lyase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 106873.62 |
Authors | Harris, P.,Poulsen, J.C.N.,Jensen, K.F.,Larsen, S. (deposition date: 2000-02-29, release date: 2000-03-15, Last modification date: 2024-03-13) |
Primary citation | Harris, P.,Poulsen, J.C.N.,Jensen, K.F.,Larsen, S. Structural basis for the catalytic mechanism of a proficient enzyme: orotidine 5'-monophosphate decarboxylase. Biochemistry, 39:4217-4224, 2000 Cited by PubMed: 10757968DOI: 10.1021/bi992952r PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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