eF-site ID 3blx-L PDB Code 3blx Chain L click to enlarge Title Yeast Isocitrate Dehydrogenase (Apo Form) Classification OXIDOREDUCTASE Compound Isocitrate dehydrogenase [NAD] subunit 1 Source null (IDH2_YEAST) Sequence L:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL Description Functional site 1) 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 2) chain L residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 3) chain L residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 4) chain L residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 5) chain L residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 6) chain L residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 7) chain L residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 8) chain L residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 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

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