6YVO
Human OMPD-domain of UMPS in complex with the substrate OMP at 1.25 Angstroms resolution, 3.55 MGy exposure
Summary for 6YVO
Entry DOI | 10.2210/pdb6yvo/pdb |
Descriptor | Uridine 5'-monophosphate synthase, OROTIDINE-5'-MONOPHOSPHATE, URIDINE-5'-MONOPHOSPHATE, ... (6 entities in total) |
Functional Keywords | ompd, omp, umps, orotidine 5'-monophosphate decarboxylase, lyase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 29733.68 |
Authors | Tittmann, K.,Rindfleisch, S.,Krull, M. (deposition date: 2020-04-28, release date: 2022-02-23, Last modification date: 2024-10-16) |
Primary citation | Rindfleisch, S.,Krull, M.,Uranga, J.,Schmidt, T.,Rabe von Pappenheim, F.,Kirck, L.L.,Balouri, A.,Schneider, T.,Chari, A.,Kluger, R.,Bourenkov, G.,Diederichsen, U.,Mata, R.A.,Tittmann, K. Ground-state destabilization by electrostatic repulsion is not a driving force in orotidine-5-monophosphate decarboxylase catalysis Nat Catal, 5:332-341, 2022 Cited by DOI: 10.1038/s41929-022-00771-wPDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.25 Å) |
Structure validation
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