eF-site ID 3blw-L PDB Code 3blw Chain L 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 L:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL Description Functional site 1) chain L residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 2) chain L residue 222 type sequence D description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 3) chain L residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 4) chain L residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 5) chain L residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 6) chain L residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 7) chain L residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 8) chain L residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 9) chain L residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain L residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain L residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain L residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain L residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 14) chain L residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 15) chain L residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7

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