eF-site ID 1a4i-AB PDB Code 1a4i Chain A, B click to enlarge Title HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE Classification OXIDOREDUCTASE Compound METHYLENETETRAHYDROFOLATE DEHYDROGENASE / METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE Source Homo sapiens (Human) (C1TC_HUMAN) Sequence A:  APAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAIL QVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEV MKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPE KDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGV PIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAH LDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYK VVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESA KRFLE B:  APAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAIL QVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEV MKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPE KDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGV PIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAH LDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV PDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVA MLMQSTVESAKRFLE Description Functional site 1) chain A residue 148 type sequence T description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 2) chain A residue 172 type sequence G description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 3) chain A residue 173 type sequence R description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 4) chain A residue 174 type sequence S description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 5) chain A residue 177 type sequence V description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 6) chain A residue 196 type sequence H description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 7) chain A residue 197 type sequence S description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 8) chain A residue 215 type sequence A description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 9) chain A residue 216 type sequence T description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 10) chain A residue 217 type sequence G description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 11) chain A residue 218 type sequence Q description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 12) chain A residue 236 type sequence C description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 13) chain A residue 237 type sequence G description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 14) chain A residue 238 type sequence I description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 15) chain A residue 276 type sequence G description BINDING SITE FOR RESIDUE NDP A 302 source : AC1 16) chain B residue 148 type sequence T description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 17) chain B residue 172 type sequence G description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 18) chain B residue 173 type sequence R description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 19) chain B residue 174 type sequence S description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 20) chain B residue 177 type sequence V description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 21) chain B residue 196 type sequence H description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 22) chain B residue 197 type sequence S description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 23) chain B residue 215 type sequence A description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 24) chain B residue 216 type sequence T description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 25) chain B residue 217 type sequence G description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 26) chain B residue 218 type sequence Q description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 27) chain B residue 221 type sequence M description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 28) chain B residue 236 type sequence C description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 29) chain B residue 237 type sequence G description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 30) chain B residue 238 type sequence I description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 31) chain B residue 279 type sequence T description BINDING SITE FOR RESIDUE NDP B 302 source : AC2 32) chain A residue 57 type catalytic sequence L description 389 source MCSA : MCSA1 33) chain A residue 101 type catalytic sequence L description 389 source MCSA : MCSA1 34) chain A residue 126 type catalytic sequence G description 389 source MCSA : MCSA1 35) chain A residue 50 type catalytic sequence N description 458 source MCSA : MCSA2 36) chain A residue 57 type catalytic sequence L description 458 source MCSA : MCSA2 37) chain A residue 101 type catalytic sequence L description 458 source MCSA : MCSA2 38) chain B residue 57 type catalytic sequence L description 389 source MCSA : MCSA3 39) chain B residue 101 type catalytic sequence L description 389 source MCSA : MCSA3 40) chain B residue 126 type catalytic sequence G description 389 source MCSA : MCSA3 41) chain B residue 50 type catalytic sequence N description 458 source MCSA : MCSA4 42) chain B residue 57 type catalytic sequence L description 458 source MCSA : MCSA4 43) chain B residue 101 type catalytic sequence L description 458 source MCSA : MCSA4 44) chain A residue 78-103 type prosite sequence ESEVMKYITSLNEDSTVHGFLVQLPL description THF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EsEVMkyItsLNeDstvhgFLVQLPL source prosite : PS00766 45) chain A residue 272-280 type prosite sequence PGGVGPMTV description THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTV source prosite : PS00767 46) chain A residue 57 type ACT_SITE sequence L description ACT_SITE => ECO:0000269|PubMed:10828945 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 57 type ACT_SITE sequence L description ACT_SITE => ECO:0000269|PubMed:10828945 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 53 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 49) chain A residue 100 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 50) chain A residue 273 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 51) chain B residue 53 type BINDING sequence I description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 52) chain B residue 100 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 53) chain B residue 273 type BINDING sequence G description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 54) chain A residue 173 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:9519408, ECO:0007744|PDB:1A4I, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB, ECO:0007744|PDB:1DIG source Swiss-Prot : SWS_FT_FI3 55) chain A residue 198 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:9519408, ECO:0007744|PDB:1A4I, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB, ECO:0007744|PDB:1DIG source Swiss-Prot : SWS_FT_FI3 56) chain B residue 173 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:9519408, ECO:0007744|PDB:1A4I, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB, ECO:0007744|PDB:1DIG source Swiss-Prot : SWS_FT_FI3 57) chain B residue 198 type BINDING sequence K description BINDING => ECO:0000269|PubMed:10828945, ECO:0000269|PubMed:9519408, ECO:0007744|PDB:1A4I, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB, ECO:0007744|PDB:1DIG source Swiss-Prot : SWS_FT_FI3 58) chain A residue 2 type MOD_RES sequence A description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI4 59) chain B residue 2 type MOD_RES sequence A description N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI4

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