eF-site ID 3blw-P PDB Code 3blw Chain P 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 P:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL Description Functional site 1) chain P residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 2) chain P residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 3) chain P residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain P residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain P residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain P residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain P residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 8) chain P residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 9) chain P residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 10) chain P residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 11) chain P residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 12) chain P residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 13) chain P residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 14) chain P residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7

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