eF-site ID 3blw-F PDB Code 3blw Chain F click to enlarge Title Yeast Isocitrate Dehydrogenase with Citrate and AMP Bound in the Regulatory Subunits Classification OXIDOREDUCTASE Compound Isocitrate dehydrogenase [NAD] subunit 1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IDH2_YEAST) Sequence F:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL Description Functional site 1) chain F residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 2) chain F residue 191 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 3) chain F residue 222 type sequence D description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 4) chain F residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 5) chain F residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 6) chain F residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 7) chain F residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 8) chain F residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 9) chain F residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 10) chain F residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain F residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain F residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain F residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain F residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 15) chain F residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 16) chain F residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links