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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 DOI10.2210/pdb6yvo/pdb
DescriptorUridine 5'-monophosphate synthase, OROTIDINE-5'-MONOPHOSPHATE, URIDINE-5'-MONOPHOSPHATE, ... (6 entities in total)
Functional Keywordsompd, omp, umps, orotidine 5'-monophosphate decarboxylase, lyase
Biological sourceHomo sapiens (Human)
Total number of polymer chains1
Total formula weight29733.68
Authors
Tittmann, K.,Rindfleisch, S.,Krull, M. (deposition date: 2020-04-28, release date: 2022-02-23, Last modification date: 2024-10-16)
Primary citationRindfleisch, 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-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.25 Å)
Structure validation

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