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4ZAL

Structure of UbiX E49Q mutant in complex with reduced FMN and dimethylallyl monophosphate

Summary for 4ZAL
Entry DOI10.2210/pdb4zal/pdb
DescriptorUbiX, Dimethylallyl monophosphate, 1-DEOXY-1-(7,8-DIMETHYL-2,4-DIOXO-3,4-DIHYDRO-2H-BENZO[G]PTERIDIN-1-ID-10(5H)-YL)-5-O-PHOSPHONATO-D-RIBITOL, ... (5 entities in total)
Functional Keywordsprenyl transferase, ubix, fmn binding, lyase
Biological sourcePseudomonas aeruginosa
Total number of polymer chains1
Total formula weight23124.39
Authors
White, M.D.,Leys, D. (deposition date: 2015-04-13, release date: 2015-06-17, Last modification date: 2015-07-01)
Primary citationWhite, M.D.,Payne, K.A.,Fisher, K.,Marshall, S.A.,Parker, D.,Rattray, N.J.,Trivedi, D.K.,Goodacre, R.,Rigby, S.E.,Scrutton, N.S.,Hay, S.,Leys, D.
UbiX is a flavin prenyltransferase required for bacterial ubiquinone biosynthesis.
Nature, 522:497-501, 2015
Cited by
PubMed: 26083743
DOI: 10.1038/nature14559
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.62 Å)
Structure validation

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