Entry Database : PDB / ID : 2cfi Structure visualization Downloads & linksTitle The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin Components10-FORMYLTETRAHYDROFOLATE DEHYDROGENASE Details Keywords OXIDOREDUCTASE / TETRAHYDROFOLATE / FOLATE BINDING / NADP / ONE-CARBON METABOLISM / PHOSPHOPANTETHEINEFunction / homology Function and homology informationFunction Domain/homology Component
formyltetrahydrofolate dehydrogenase / formyltetrahydrofolate dehydrogenase activity / 10-formyltetrahydrofolate catabolic process / NADPH regeneration / Metabolism of folate and pterines / aldehyde dehydrogenase (NAD+) activity / biosynthetic process / one-carbon metabolic process / extracellular exosome / cytosol Similarity search - Function Formyl transferase, C-terminal domain / Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2 / 10-formyltetrahydrofolate dehydrogenase / Formyl transferase, C-terminal domain superfamily / Formyl transferase, C-terminal / Formyl transferase, C-terminal domain / Formyl transferase-like, C-terminal domain superfamily / Formyl transferase, N-terminal domain / Phosphoribosylglycinamide formyltransferase, active site / Phosphoribosylglycinamide formyltransferase active site. ... Formyl transferase, C-terminal domain / Methionyl-tRNA Fmet Formyltransferase; Chain A, domain 2 / 10-formyltetrahydrofolate dehydrogenase / Formyl transferase, C-terminal domain superfamily / Formyl transferase, C-terminal / Formyl transferase, C-terminal domain / Formyl transferase-like, C-terminal domain superfamily / Formyl transferase, N-terminal domain / Phosphoribosylglycinamide formyltransferase, active site / Phosphoribosylglycinamide formyltransferase active site. / Formyl transferase, N-terminal / Formyl transferase / Formyl transferase, N-terminal domain superfamily / Aldehyde dehydrogenase, glutamic acid active site / Aldehyde dehydrogenases glutamic acid active site. / Aldehyde dehydrogenase, cysteine active site / Aldehyde dehydrogenases cysteine active site. / Aldehyde dehydrogenase domain / Aldehyde dehydrogenase family / Aldehyde dehydrogenase, N-terminal / Aldehyde dehydrogenase, C-terminal / Aldehyde/histidinol dehydrogenase / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Roll / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species HOMO SAPIENS (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.85 Å DetailsAuthors Kursula, P. / Stenmark, P. / Arrowsmith, C. / Edwards, A. / Ehn, M. / Graslund, S. / Hammarstrom, M. / Hallberg, M. / Kotenyova, T. / Nilsson-Ehle, P. ...Kursula, P. / Stenmark, P. / Arrowsmith, C. / Edwards, A. / Ehn, M. / Graslund, S. / Hammarstrom, M. / Hallberg, M. / Kotenyova, T. / Nilsson-Ehle, P. / Nordlund, P. / Ogg, D.J. / Persson, C. / Sagemark, J. / Schuler, H. / Sundstrom, M. / Thorsell, A. / Weigelt, J. CitationJournal : Acta Crystallogr.,Sect.D / Year : 2006Title : Structures of the Hydrolase Domain of Human 10-Formyltetrahydrofolate Dehydrogenase and its Complex with a Substrate Analogue.Authors : Kursula, P. / Schuler, H. / Flodin, S. / Nilsson-Ehle, P. / Ogg, D.J. / Savitsky, P. / Nordlund, P. / Stenmark, P. History Deposition Feb 21, 2006 Deposition site : PDBE / Processing site : PDBERevision 1.0 Mar 14, 2006 Provider : repository / Type : Initial releaseRevision 1.1 Jul 13, 2011 Group : Advisory / Version format complianceRevision 1.2 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.