eF-site ID 1dia-B PDB Code 1dia Chain B click to enlarge Title HUMAN METHYLENETETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE COMPLEXED WITH NADP AND INHIBITOR LY249543 Classification OXIDOREDUCTASE,HYDROLASE Compound METHYLENETETRAHYDROFOLATE DEHYDROGENASE/CYCLOHYDROLASE Source null (C1TC_HUMAN) Sequence B:  APAEILNGKEISAQIRARLKNQVTQLKEQVPGFTPRLAIL QVGNRDDSNLYINVKLKAAEEIGIKATHIKLPRTTTESEV MKYITSLNEDSTVHGFLVQLPLDSENSINTEEVINAIAPE KDVDGLTSINAGRLARGDLNDCFIPCTPKGCLELIKETGV PIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTAH LDEEVNKGDILVVATGQPEMVKGEWIKPGAIVIDCGINYV PDDKKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVA MLMQSTVESAKRFLE Description Functional site 1) chain B residue 1148 type sequence T description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 2) chain B residue 1173 type sequence R description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 3) chain B residue 1174 type sequence S description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 4) chain B residue 1196 type sequence H description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 5) chain B residue 1197 type sequence S description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 6) chain B residue 1216 type sequence T description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 7) chain B residue 1217 type sequence G description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 8) chain B residue 1218 type sequence Q description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 9) chain B residue 1221 type sequence M description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 10) chain B residue 1236 type sequence C description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 11) chain B residue 1238 type sequence I description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 12) chain B residue 1276 type sequence G description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 13) chain B residue 1279 type sequence T description BINDING SITE FOR RESIDUE NAP B 2002 source : AC2 14) chain B residue 1056 type catalytic sequence K description 389 source MCSA : MCSA3 15) chain B residue 1100 type catalytic sequence Q description 389 source MCSA : MCSA3 16) chain B residue 1125 type catalytic sequence D description 389 source MCSA : MCSA3 17) chain B residue 1049 type catalytic sequence S description 458 source MCSA : MCSA4 18) chain B residue 1056 type catalytic sequence K description 458 source MCSA : MCSA4 19) chain B residue 1100 type catalytic sequence Q description 458 source MCSA : MCSA4 20) chain B residue 1056 type ACT_SITE sequence K description ACT_SITE => ECO:0000269|PubMed:10828945 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 1052 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 22) chain B residue 1099 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 23) chain B residue 1272 type BINDING sequence P description BINDING => ECO:0000269|PubMed:10828945, ECO:0007744|PDB:1DIA, ECO:0007744|PDB:1DIB source Swiss-Prot : SWS_FT_FI2 24) chain B residue 1172 type BINDING sequence G 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 25) chain B residue 1197 type BINDING sequence S 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

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