eF-site ID 3blx-ABCDEFGHIJKLMNOP PDB Code 3blx Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P Title Yeast Isocitrate Dehydrogenase (Apo Form) Classification OXIDOREDUCTASE Compound Isocitrate dehydrogenase [NAD] subunit 1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (IDH2_YEAST) Sequence A:  KYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETI NIKQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGS LNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENT EGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKK YNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVS SIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIG GPGLVAGANFGRDYAVFEPGSRHVGLKGQNVANPTAMILS STLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSS TTDFTNEIINKLSTM B:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL C:  RTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPI DWETINIKQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQ TGHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIV IRENTEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAF DFAKKYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYP DIDVSSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIG AALIGGPGLVAGANFGRDYAVFEPGSRHVKGQNVANPTAM ILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGG SSSTTDFTNEIINKLSTM D:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL E:  RTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPI DWETINIKQDHKEGVYEAVESLKRNKIGLKGLWHTPADQT GHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVI RENTEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFD FAKKYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPD IDVSSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGA ALIGGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANP TAMILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRD IGGSSSTTDFTNEIINKLSTM F:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL G:  KYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETI NIKQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGS LNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENT EGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKK YNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVS SIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIG GPGLVAGANFGRDYAVFEPGSRHVGKGQNVANPTAMILSS TLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSST TDFTNEIINKLSTM H:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL I:  RFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINIKQ TDHKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVA LRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEF SGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRK SVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIV DNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGL VAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSST LMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTT DFTNEIINKLSTM J:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL K:  RTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPI DWETINIKQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQ TGHGSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIV IRENTEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAF DFAKKYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYP DIDVSSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIG AALIGGPGLVAGANFGRDYAVFEPGSRHVKGQNVANPTAM ILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGG SSSTTDFTNEIINKLSTM L:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL M:  RTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPI DWETINIKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGS LNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENT EGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKK YNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVS SIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIG GPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAMI LSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGS SSTTDFTNEIINKLSTM N:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENV DLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVI RYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSK EYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDI LSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAG QDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIASG PENRTGDLAGTATTSSFTEAVIKRL O:  GGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINI KQTDHKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLN VALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEG EFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKKYN RKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSI IVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGP GLVAGANFGRDYAVFEPGSRHVGKGQNVANPTAMILSSTL MLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTD FTNEIINKLSTM P:  TVSFIEGDGIGPEISKSVKKIFSAANVPIEWESCDVSPIF VNGLTTIPDPAVQSITKNLVALKGPLATRSLNLTLRKTFG LFANVRPAKSIEGFKTTYENVDLVLIRENTEGEYSGIEHI VCPGVVQSIKLITRDASERVIRYAFEYARAIGRPRVIVVH KSTIQRLADGLFVNVAKELSKEYPDLTLETELIDNSVLKV VTNPSAYTDAVSVCPNLYGDILSDLNSGLSAGSLGLTPSA NIGHKISIFEAVHGSAPDIAGQDKANPTALLLSSVMMLNH MGLTNHADQIQNAVLSTIASGPENRTGDLAGTATTSSFTE AVIKRL Description Functional site 1) chain A residue 237-256 type prosite sequence SMYGTILGNIGAALIGGPGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. SMYGTIlGNigAali.GGPGL source prosite : PS00470 2) chain B residue 244-264 type prosite sequence NLYGDILSDLNSGLSAGSLGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. SMYGTIlGNigAali.GGPGL source prosite : PS00470 3) chain B residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 4) chain F residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 5) chain F residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 7) chain H residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 8) chain H residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 9) chain H residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 10) chain H residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 11) chain J residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 12) chain J residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 13) chain J residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 15) chain J residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 16) chain L residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 17) chain L residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 18) chain L residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 19) chain L residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 20) chain N residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 21) chain N residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 22) chain N residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 23) chain N residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 24) chain P residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain P residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 27) chain P residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 28) chain P residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 30) chain D residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 31) chain D residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 32) chain D residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 33) chain D residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 34) chain F residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 36) chain J residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 37) chain L residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 38) chain L residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 39) chain N residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 40) chain N residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 41) chain P residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 42) chain P residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 44) chain D residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 45) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 46) chain F residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 47) chain F residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 48) chain H residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 49) chain H residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 50) chain J residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 51) chain B residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 52) chain J residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 53) chain L residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 54) chain L residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 55) chain N residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 56) chain N residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 57) chain P residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 58) chain P residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 59) chain B residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 60) chain D residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 61) chain D residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 62) chain F residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 63) chain F residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 64) chain H residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 65) chain H residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 66) chain J residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 67) chain B residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 68) chain D residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 69) chain F residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 70) chain H residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 71) chain J residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 72) chain L residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 73) chain N residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 74) chain P residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 75) 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 76) 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 77) 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 78) 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 79) chain J residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 80) 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 81) chain N residue 138 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 82) 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 83) chain B residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 84) chain D residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 85) chain F residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 86) chain H residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 87) chain J residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 88) chain L residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 89) chain N residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 90) chain P residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 91) chain B residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 92) chain D residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 93) chain F residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 94) chain H residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 95) chain J residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 96) chain L residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 97) chain N residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 98) chain P residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links