1A4I

HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE

Summary for 1A4I

• Entry DOI: 10.2210/pdb1a4i/pdb
• Descriptor: METHYLENETETRAHYDROFOLATE DEHYDROGENASE / METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: thf, bifunctional, dehydrogenase, cyclohydrolase, folate, oxidoreductase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P11586
• Total number of polymer chains: 2
• Total formula weight: 66791.93

Authors

Allaire, M.,Li, Y.,Mackenzie, R.E.,Cygler, M. (deposition date: 1998-01-30, release date: 1999-02-09, Last modification date: 2024-02-07)

Primary citation

Allaire, M.,Li, Y.,MacKenzie, R.E.,Cygler, M.
The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution.
Structure, 6:173-182, 1998

PubMed Abstract: The interconversion of two major folate one-carbon donors occurs through the sequential activities of NAD(P)-dependent methylene[H4]folate dehydrogenase (D) and methenyl[H4]folate cyclohydrolase (C). These activities often coexist as part of a multifunctional enzyme and there are several lines of evidence suggesting that their substrates bind at overlapping sites. Little is known, however, about the nature of this site or the identity of the active-site residues for this enzyme family.

PubMed: 9519408
DOI: 10.1016/S0969-2126(98)00019-7

Experimental method

X-RAY DIFFRACTION (1.5 Å)