3LHW
Crystal structure of the mutant V182A of orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with inhibitor BMP
Summary for 3LHW
Entry DOI | 10.2210/pdb3lhw/pdb |
Related | 3LHT 3LHU 3LHV 3LHY 3LHZ 3LI0 3LI1 |
Descriptor | Orotidine 5'-phosphate decarboxylase, 1-(5'-PHOSPHO-BETA-D-RIBOFURANOSYL)BARBITURIC ACID (3 entities in total) |
Functional Keywords | mutant v182a, 6-hydroxyuridine-5'-phosphate, decarboxylase, pyrimidine biosynthesis, lyase |
Biological source | Methanothermobacter thermautotrophicus |
Total number of polymer chains | 2 |
Total formula weight | 50393.65 |
Authors | Fedorov, A.A.,Fedorov, E.V.,Wood, B.M.,Gerlt, J.A.,Almo, S.C. (deposition date: 2010-01-23, release date: 2010-06-16, Last modification date: 2023-09-06) |
Primary citation | Wood, B.M.,Amyes, T.L.,Fedorov, A.A.,Fedorov, E.V.,Shabila, A.,Almo, S.C.,Richard, J.P.,Gerlt, J.A. Conformational changes in orotidine 5'-monophosphate decarboxylase: "remote" residues that stabilize the active conformation. Biochemistry, 49:3514-3516, 2010 Cited by PubMed: 20369850DOI: 10.1021/bi100443a PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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