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1EIX

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP

Summary for 1EIX
Entry DOI10.2210/pdb1eix/pdb
DescriptorOROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE, 1-(5'-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC ACID (3 entities in total)
Functional Keywordsalpha-beta-barrel, protein-inhibitor complex, homodimer, lyase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight106873.62
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 citationHarris, 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: 10757968
DOI: 10.1021/bi992952r
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

217705

数据于2024-03-27公开中

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