5CCC
wild-type E.coli dihydrofolate reductase complexed with 5,10-dideazatetrahydrofolate and oxidized nicotinamide adenine dinucleotide phosphate
Summary for 5CCC
Entry DOI | 10.2210/pdb5ccc/pdb |
Related | 5CC9 |
Descriptor | Dihydrofolate reductase, 5,10-DIDEAZATETRAHYDROFOLIC ACID, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
Functional Keywords | folate metabolism, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 19206.20 |
Authors | Oyen, D.,Wright, P.E. (deposition date: 2015-07-01, release date: 2015-08-05, Last modification date: 2023-09-27) |
Primary citation | Oyen, D.,Fenwick, R.B.,Stanfield, R.L.,Dyson, H.J.,Wright, P.E. Cofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway. J.Am.Chem.Soc., 137:9459-9468, 2015 Cited by PubMed: 26147643DOI: 10.1021/jacs.5b05707 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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