1B5T
ESCHERICHIA COLI METHYLENETETRAHYDROFOLATE REDUCTASE
Summary for 1B5T
Entry DOI | 10.2210/pdb1b5t/pdb |
Descriptor | PROTEIN (METHYLENETETRAHYDROFOLATE REDUCTASE), MERCURY (II) ION, FLAVIN-ADENINE DINUCLEOTIDE, ... (4 entities in total) |
Functional Keywords | beta alpha barrel, reductase, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 3 |
Total formula weight | 95304.73 |
Authors | Guenther, B.D.,Sheppard, C.A.,Tran, P.,Rozen, R.,Matthews, R.G.,Ludwig, M.L. (deposition date: 1999-01-07, release date: 1999-01-20, Last modification date: 2024-02-07) |
Primary citation | Guenther, B.D.,Sheppard, C.A.,Tran, P.,Rozen, R.,Matthews, R.G.,Ludwig, M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat.Struct.Biol., 6:359-365, 1999 Cited by PubMed: 10201405DOI: 10.1038/7594 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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