eF-site ID 3blw-ABCDEFGHIJKLMNOP PDB Code 3blw Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P 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 A:  GRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINIK EGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALRKQ LDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSGLE HESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRKSVTA VHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIVDNAS MQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGLVAGA NFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLN HLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDFTN EIINKLSTM B:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL C:  ERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIP IDWETINIKEGVYEAVESLKRNKIGLKGLWHTPADQTGHG SLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIREN TEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAK KYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDV SSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALI GGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAM ILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGG SSSTTDFTNEIINKLSTM D:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL E:  ERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIP IDWETINIKEGVYEAVESLKRNKIGLKGLWHTPADQTGHG SLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIREN TEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAK KYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDV SSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALI GGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAM ILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGG SSSTTDFTNEIINKLSTM F:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL G:  GRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINIK EGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALRKQ LDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSGLE HESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRKSVTA VHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIVDNAS MQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGLVAGA NFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLN HLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDFTN EIINKLSTM H:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL I:  GRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINIK EGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALRKQ LDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSGLE HESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRKSVTA VHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIVDNAS MQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGLVAGA NFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLMLN HLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDFTN EIINKLSTM J:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL K:  RTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENIPI DWETINIKEGVYEAVESLKRNKIGLKGLWHTPADQTGHGS LNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRENT EGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFAKK YNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDIDVS SIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAALIG GPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTAMI LSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIGGS SSTTDFTNEIINKLSTM L:  QPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIF SAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVAL KGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYEN VDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERV IRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELS KEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGD ILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIA GQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIAS GPENRTGDLAGTATTSSFTEAVIKRL M:  AERTLPKKYGGRFTVTLIPGDGVGKEITDSVRTIFEAENI PIDWETINIKEGVYEAVESLKRNKIGLKGLWHTPADQTGH GSLNVALRKQLDIYANVALFKSLKGVKTRIPDIDLIVIRE NTEGEFSGLEHESVPGVVESLKVMTRPKTERIARFAFDFA KKYNRKSVTAVHKANIMKLGDGLFRNIITEIGQKEYPDID VSSIIVDNASMQAVAKPHQFDVLVTPSMYGTILGNIGAAL IGGPGLVAGANFGRDYAVFEPGSRHVGLDIKGQNVANPTA MILSSTLMLNHLGLNEYATRISKAVHETIAEGKHTTRDIG GSSSTTDFTNEIINKLSTM N:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL O:  GGRFTVTLIPGDGVGKEITDSVRTIFEAENIPIDWETINI KEGVYEAVESLKRNKIGLKGLWHTPADQTGHGSLNVALRK QLDIYANVALFKSLKGVKTRIPDIDLIVIRENTEGEFSGL EHESVPGVVESLKVMTRPKTERIARFAFDFAKKYNRKSVT AVHKANIMKLGDGLFRNIITEIGQKEYPDIDVSSIIVDNA SMQAVAKPHQFDVLVTPSMYGTILGNIGAALIGGPGLVAG ANFGRDYAVFEPGSRHVGLDIKGQNVANPTAMILSSTLML NHLGLNEYATRISKAVHETIAEGKHTTRDIGGSSSTTDFT NEIINKLSTM P:  KQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKI FSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVA LKGPLATPHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYE NVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASER VIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKEL SKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYG DILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDI AGQDKANPTALLLSSVMMLNHMGLTNHADQIQNAVLSTIA SGPENRTGDLAGTATTSSFTEAVIKRL 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 95 type sequence V description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 5) chain A residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 6) chain A residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 7) chain A residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 8) chain A residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 9) chain A residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 10) chain B residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC A 1001 source : AC1 11) chain C residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 12) chain C residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 13) chain C residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 14) chain C residue 95 type sequence V description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 15) chain C residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 16) chain C residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 17) chain C residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 18) chain C residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 19) chain C residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 20) chain D residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC C 1002 source : AC2 21) chain E residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 22) chain E residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 23) chain E residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 24) chain E residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 25) chain E residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 26) chain E residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 27) chain E residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 28) chain F residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 29) chain F residue 191 type sequence T description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 30) chain F residue 222 type sequence D description BINDING SITE FOR RESIDUE FLC E 1003 source : AC3 31) chain G residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 32) chain G residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 33) chain G residue 95 type sequence V description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 34) chain G residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 35) chain G residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 36) chain G residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 37) chain G residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 38) chain G residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 39) chain H residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 40) chain H residue 191 type sequence T description BINDING SITE FOR RESIDUE FLC G 1004 source : AC4 41) chain I residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 42) chain I residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 43) chain I residue 95 type sequence V description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 44) chain I residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 45) chain I residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 46) chain I residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 47) chain I residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 48) chain I residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 49) chain J residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC I 1005 source : AC5 50) chain K residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 51) chain K residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 52) chain K residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 53) chain K residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 54) chain K residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 55) chain K residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 56) chain K residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 57) chain L residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 58) chain L residue 222 type sequence D description BINDING SITE FOR RESIDUE FLC K 1006 source : AC6 59) chain M residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 60) chain M residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 61) chain M residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 62) chain M residue 95 type sequence V description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 63) chain M residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 64) chain M residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 65) chain M residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 66) chain M residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 67) chain N residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC M 1007 source : AC7 68) chain O residue 83 type sequence T description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 69) chain O residue 92 type sequence S description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 70) chain O residue 94 type sequence N description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 71) chain O residue 98 type sequence R description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 72) chain O residue 129 type sequence R description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 73) chain O residue 136 type sequence F description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 74) chain O residue 241 type sequence T description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 75) chain O residue 274 type sequence R description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 76) chain P residue 189 type sequence K description BINDING SITE FOR RESIDUE FLC O 1008 source : AC8 77) chain A residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 78) chain A residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 79) chain A residue 286 type sequence A description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 80) chain A residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 81) chain A residue 328 type sequence D description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 82) chain B residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP A 2001 source : AC9 83) chain C residue 28 type sequence V description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 84) chain C residue 32 type sequence I description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 85) chain C residue 255 type sequence G description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 86) chain C residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 87) chain C residue 276 type sequence V description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 88) chain C residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 89) chain C residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 90) chain D residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP C 2002 source : BC1 91) chain E residue 28 type sequence V description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 92) chain E residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 93) chain E residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 94) chain E residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 95) chain F residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP E 2003 source : BC2 96) chain G residue 28 type sequence V description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 97) chain G residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 98) chain G residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 99) chain G residue 286 type sequence A description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 100) chain G residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 101) chain G residue 328 type sequence D description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 102) chain H residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP G 2004 source : BC3 103) chain I residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 104) chain I residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 105) chain I residue 286 type sequence A description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 106) chain I residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 107) chain I residue 328 type sequence D description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 108) chain J residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP I 2005 source : BC4 109) chain K residue 28 type sequence V description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 110) chain K residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 111) chain K residue 276 type sequence V description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 112) chain K residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 113) chain K residue 286 type sequence A description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 114) chain L residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP K 2006 source : BC5 115) chain M residue 32 type sequence I description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 116) chain M residue 255 type sequence G description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 117) chain M residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 118) chain M residue 276 type sequence V description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 119) chain M residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 120) chain M residue 279 type sequence D description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 121) chain M residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 122) chain N residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP M 2007 source : BC6 123) chain O residue 28 type sequence V description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 124) chain O residue 275 type sequence H description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 125) chain O residue 276 type sequence V description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 126) chain O residue 277 type sequence G description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 127) chain O residue 287 type sequence N description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 128) chain O residue 328 type sequence D description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 129) chain P residue 223 type sequence N description BINDING SITE FOR RESIDUE AMP O 2008 source : BC7 130) chain B residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 131) chain J residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 132) chain L residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 133) chain L residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 134) chain N residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 135) chain N residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 136) chain P residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 137) chain P residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 138) chain B residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 139) chain D residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 140) chain D residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 141) chain F residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 142) chain F residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 143) chain H residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 144) chain H residue 189 type SITE sequence K description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 145) chain J residue 142 type SITE sequence Y description Critical for catalysis => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 146) chain B residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 147) chain D residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 148) chain F residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 149) chain H residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 150) chain J residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 151) chain L residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 152) chain N residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 153) chain P residue 90 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4 154) chain B residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 155) chain J residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 156) chain L residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 157) chain L residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 158) chain N residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 159) chain N residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 160) chain P residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 161) chain P residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 162) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 163) chain D residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 164) chain D residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 165) chain F residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 166) chain F residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 167) chain H residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 168) chain H residue 252 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 169) chain J residue 248 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P50213 source Swiss-Prot : SWS_FT_FI2 170) chain B residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 171) chain F residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 172) chain F residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 173) chain F residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 174) chain H residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 175) chain H residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 176) chain H residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 177) chain H residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 178) chain J residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 179) chain J residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 180) chain J residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 181) chain B residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 182) chain J residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 183) chain L residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 184) chain L residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 185) chain L residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 186) chain L residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 187) chain N residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 188) chain N residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 189) chain N residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 190) chain N residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 191) chain P residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 192) chain B residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 193) chain P residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 194) chain P residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 195) chain P residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 196) chain B residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 197) chain D residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 198) chain D residue 114 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 199) chain D residue 135 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 200) chain D residue 222 type BINDING sequence D description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 201) chain F residue 104 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 202) 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 203) 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 204) 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 205) 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 206) 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 207) 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 208) 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 209) 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 210) chain B residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 211) chain D residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 212) chain F residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 213) chain H residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 214) chain J residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 215) chain L residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 216) chain N residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 217) chain P residue 312 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 218) chain B residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 219) chain D residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 220) chain F residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 221) chain H residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 222) chain J residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 223) chain L residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 224) chain N residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 225) chain P residue 334 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:17761666 source Swiss-Prot : SWS_FT_FI7 226) chain B residue 244-264 type prosite sequence NLYGDILSDLNSGLSAGSLGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlnSglsaGSLGL source prosite : PS00470 227) chain A residue 237-256 type prosite sequence SMYGTILGNIGAALIGGPGL description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLYGDIlSDlnSglsaGSLGL source prosite : PS00470

Display surface Download Links