eF-site ID 3blv-ABCDEFGH PDB Code 3blv Chain A, B, C, D, E, F, G, H click to enlarge Title Yeast Isocitrate Dehydrogenase with Citrate 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 A:  YGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETIN IKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALR KQLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSG LEHESVPGVVESLKVXTRPKTERIARFAFDFAKKYNRKSV TAVHKANIXKLGDGLFRNIITEIGQKEYPDIDVSSIIVDN ASXQAVAKPHQFDVLVTPSXYGTILGNIGAALIGGPGLVA GANFGRDYAVFEPGSRHVGLDIKGQNVANPTAXILSSTLX LNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDF TNEIINKLSTX B:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVXXLNHXGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL C:  ATAAQAERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIF EAENIPIDWETINIKEGVYEAVESLKRNKIGLKGLWHTPA DQTGHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDL IVIRENTEGEFSGLEHESVPGVVESLKVXTRPKTERIARF AFDFAKKYNRKSVTAVHKANIXKLGDGLFRNIITEIGQKE YPDIDVSSIIVDNASXQAVAKPHQFDVLVTPSXYGTILGN IGAALIGGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNV ANPTAXILSSTLXLNHLGLNEYATRISKAVHETIAEGKHT TRDIGGSSSTTDFTNEIINKLSTX D:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVXXLNHXGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL E:  ATAAQAERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIF EAENIPIDWETINIKEGVYEAVESLKRNKIGLKGLWHTPA DQTGHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDL IVIRENTEGEFSGLEHESVPGVVESLKVXTRPKTERIARF AFDFAKKYNRKSVTAVHKANIXKLGDGLFRNIITEIGQKE YPDIDVSSIIVDNASXQAVAKPHQFDVLVTPSXYGTILGN IGAALIGGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNV ANPTAXILSSTLXLNHLGLNEYATRISKAVHETIAEGKHT TRDIGGSSSTTDFTNEIINKLSTX F:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVXXLNHXGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL G:  YGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETIN IKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALR KQLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSG LEHESVPGVVESLKVXTRPKTERIARFAFDFAKKYNRKSV TAVHKANIXKLGDGLFRNIITEIGQKEYPDIDVSSIIVDN ASXQAVAKPHQFDVLVTPSXYGTILGNIGAALIGGPGLVA GANFGRDYAVFEPGSRHVGLDIKGQNVANPTAXILSSTLX LNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDF TNEIINKLSTX H:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPIGRSLNLTLRKTFGLFANVRPAKSIEGFKTTY ENVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASE RVIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKE LSKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLY GDILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPD IAGQDKANPTALLLSSVXXLNHXGLTNHADQIQNAVLSTI ASGPENRTGDLAGTATTSSFTEAVIKRL Description Functional site 1) chain A residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 2) chain A residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 3) chain A residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 4) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 5) chain A residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 6) chain A residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 7) chain A residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 8) chain A residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 9) chain B residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 10) chain C residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 11) chain C residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 12) chain C residue 95 type sequence V description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 13) chain C residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 14) chain C residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 15) chain C residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 16) chain C residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 17) chain C residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 18) chain D residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 19) chain E residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 20) chain E residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 21) chain E residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 22) chain E residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 23) chain E residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 24) chain E residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 25) chain E residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 26) chain E residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 27) chain F residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 28) chain G residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 29) chain G residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 30) chain G residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 31) chain G residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 32) chain G residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 33) chain G residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 34) chain G residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 35) chain G residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 36) chain H residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 37) chain H residue 191 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 38) chain B residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 40) chain D residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 41) chain D residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 42) chain F residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 43) chain F residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 44) chain H residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 45) chain H residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 46) chain B residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 47) chain D residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 48) chain F residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 49) chain H residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 52) chain D residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 53) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 54) chain F residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 55) chain F residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 56) chain H residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 57) chain H residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 58) chain B residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 59) chain F residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 60) chain F residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 61) chain F residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 62) chain H residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 63) chain H residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 64) chain H residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 65) chain H residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 66) chain B residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 67) chain B residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 69) chain D residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 70) chain D residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 71) chain D residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 72) chain D residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 73) chain F residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 75) chain D residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 76) 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 77) chain H residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 78) chain B residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 79) chain D residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 80) chain F residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 81) chain H residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 82) chain B residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 83) chain D residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 84) chain F residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 85) chain H residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 86) chain B residue 244-264 type prosite sequence NLYGDILSDLNSGLSAGSLGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlnSglsaGSLGL source prosite : PS00470 87) chain A residue 237-256 type prosite sequence SXYGTILGNIGAALIGGPGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlnSglsaGSLGL source prosite : PS00470

Display surface Download Links