eF-site ID 3lcb-ABCD PDB Code 3lcb Chain A, B, C, D click to enlarge Title The crystal structure of isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli. Classification TRANSFERASE, HYDROLASE Compound Isocitrate dehydrogenase kinase/phosphatase Source Escherichia coli O157:H7 (strain EC4115 / EHEC) (IDH_ECOLI) Sequence A:  GLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAV QQAMKNRIHLYDHHVGLVVEQLRCITNEFLLRVKEHYTRL LPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPR PLAKDFHPDHGWESLLMRVISDLPLRLHWQNKSRDIHYII RHLTETLGPENLSKSHLQVANELFYRNKAAWLVGKLITPS GTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYF MVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTES YREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKV IKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFEN FVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIER RMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGD MLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPE DELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHA DLFRADYWRALQNRIREGHVEDVYAYRRRQRFSV B:  LELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQ QAMKNRIHLYDHHVGLVVEQLRCITNEFLLRVKEHYTRLL PDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPER RFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLHWQNKS RDIHYIIRHLTETLGPENLSKSHLQVANELFYRNKAAWLV GKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVF GFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQ KHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPG FDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMA DTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVI RHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAA ANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDI PPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGP LFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFS V C:  ESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDV TPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQD VWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQE LDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYA GIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPC SEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAF KDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVI ADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIG IAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAE MMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAK LLKCSEFGDAIIENM D:  ESKVVVPAQGKKITLQNGKLNVPENPIIPYIEGDGIGVDV TPAMLKVVDAAVEKAYKGERKISWMEIYTGEKSTQVYGQD VWLPAETLDLIREYRVAIKGPLTTPVGGGIRSLNVALRQE LDLYICLRPVRYYQGTPSPVKHPELTDMVIFRENSEDIYA GIEWKADSADAEKVIKFLREEMGVKKIRFPEHCGIGIKPC SEEGTKRLVRAAIEYAIANDRDSVTLVHKGNIMKFTEGAF KDWGYQLAREEFGGELIDGGPWLKVKNPNTGKEIVIKDVI ADAFLQQILLRPAEYDVIACMNLNGDYISDALAAQVGGIG IAPGANIGDECALFEATHGTAPKYAGQDKVNPGSIILSAE MMLRHMGWTEAADLIVKGMEGAINAKTVTYDFERLMDGAK LLKCSEFGDAIIENM Description Functional site 1) chain A residue 104 type sequence N description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 2) chain A residue 105 type sequence S description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 3) chain A residue 113 type sequence H description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 4) chain A residue 116 type sequence L description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 5) chain A residue 291 type sequence K description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 6) chain A residue 294 type sequence K description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 7) chain A residue 295 type sequence T description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 8) chain A residue 298 type sequence Y description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 9) chain A residue 375 type sequence F description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 10) chain A residue 376 type sequence E description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 11) chain A residue 377 type sequence N description BINDING SITE FOR RESIDUE AMP A 1604 source : AC1 12) chain A residue 316 type sequence P description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 13) chain A residue 317 type sequence G description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 14) chain A residue 318 type sequence I description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 15) chain A residue 320 type sequence G description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 16) chain A residue 321 type sequence M description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 17) chain A residue 322 type sequence V description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 18) chain A residue 323 type sequence M description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 19) chain A residue 325 type sequence V description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 20) chain A residue 334 type sequence V description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 21) chain A residue 336 type sequence K description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 22) chain A residue 346 type sequence K description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 23) chain A residue 416 type sequence E description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 24) chain A residue 417 type sequence R description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 25) chain A residue 419 type sequence M description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 26) chain A residue 421 type sequence P description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 27) chain A residue 457 type sequence D description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 28) chain A residue 461 type sequence K description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 29) chain A residue 462 type sequence N description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 30) chain A residue 474 type sequence Y description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 31) chain A residue 475 type sequence D description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 32) chain A residue 477 type sequence D description BINDING SITE FOR RESIDUE ATP A 1760 source : AC2 33) chain A residue 462 type sequence N description BINDING SITE FOR RESIDUE MG A 579 source : AC3 34) chain A residue 475 type sequence D description BINDING SITE FOR RESIDUE MG A 579 source : AC3 35) chain B residue 316 type sequence P description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 36) chain B residue 318 type sequence I description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 37) chain B residue 320 type sequence G description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 38) chain B residue 321 type sequence M description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 39) chain B residue 322 type sequence V description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 40) chain B residue 323 type sequence M description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 41) chain B residue 325 type sequence V description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 42) chain B residue 334 type sequence V description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 43) chain B residue 336 type sequence K description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 44) chain B residue 346 type sequence K description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 45) chain B residue 416 type sequence E description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 46) chain B residue 417 type sequence R description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 47) chain B residue 419 type sequence M description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 48) chain B residue 457 type sequence D description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 49) chain B residue 461 type sequence K description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 50) chain B residue 462 type sequence N description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 51) chain B residue 474 type sequence Y description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 52) chain B residue 475 type sequence D description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 53) chain B residue 477 type sequence D description BINDING SITE FOR RESIDUE ATP B 1761 source : AC4 54) chain B residue 104 type sequence N description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 55) chain B residue 105 type sequence S description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 56) chain B residue 113 type sequence H description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 57) chain B residue 116 type sequence L description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 58) chain B residue 291 type sequence K description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 59) chain B residue 294 type sequence K description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 60) chain B residue 295 type sequence T description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 61) chain B residue 298 type sequence Y description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 62) chain B residue 375 type sequence F description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 63) chain B residue 376 type sequence E description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 64) chain B residue 377 type sequence N description BINDING SITE FOR RESIDUE AMP B 1604 source : AC5 65) chain B residue 462 type sequence N description BINDING SITE FOR RESIDUE MG B 579 source : AC6 66) chain B residue 475 type sequence D description BINDING SITE FOR RESIDUE MG B 579 source : AC6 67) chain C residue 160 type catalytic sequence Y description 7 source MCSA : MCSA1 68) chain C residue 230 type catalytic sequence K description 7 source MCSA : MCSA1 69) chain C residue 283 type catalytic sequence D description 7 source MCSA : MCSA1 70) chain C residue 307 type catalytic sequence D description 7 source MCSA : MCSA1 71) chain D residue 160 type catalytic sequence Y description 7 source MCSA : MCSA2 72) chain D residue 230 type catalytic sequence K description 7 source MCSA : MCSA2 73) chain D residue 283 type catalytic sequence D description 7 source MCSA : MCSA2 74) chain D residue 307 type catalytic sequence D description 7 source MCSA : MCSA2 75) chain C residue 104 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR source Swiss-Prot : SWS_FT_FI1 76) chain D residue 104 type BINDING sequence T description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR source Swiss-Prot : SWS_FT_FI1 77) chain C residue 113 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144 source Swiss-Prot : SWS_FT_FI10 78) chain D residue 113 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:3112144 source Swiss-Prot : SWS_FT_FI10 79) chain C residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI11 80) chain D residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:18723842 source Swiss-Prot : SWS_FT_FI11 81) chain C residue 113 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 82) chain C residue 115 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 83) chain C residue 129 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 84) chain C residue 153 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 85) chain D residue 113 type BINDING sequence S description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 86) chain D residue 115 type BINDING sequence N description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 87) chain D residue 129 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 88) chain D residue 153 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW1, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI2 89) chain C residue 119 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI3 90) chain D residue 119 type BINDING sequence R description BINDING => ECO:0000269|PubMed:10623532, ECO:0000269|PubMed:2204109, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1CW7, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:1PB1, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJA, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:5ICD, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI3 91) chain C residue 307 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDC, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI4 92) chain D residue 307 type BINDING sequence D description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2204109, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI3, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1GRP, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDC, ECO:0007744|PDB:1P8F, ECO:0007744|PDB:4AJB, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:4AJS, ECO:0007744|PDB:4BNP, ECO:0007744|PDB:8ICD source Swiss-Prot : SWS_FT_FI4 93) chain C residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:1ISO, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI5 94) chain D residue 339 type BINDING sequence H description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:1ISO, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI5 95) chain C residue 352 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI6 96) chain C residue 391 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI6 97) chain D residue 352 type BINDING sequence N description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI6 98) chain D residue 391 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:1BL5, ECO:0007744|PDB:1HJ6, ECO:0007744|PDB:1IDE, ECO:0007744|PDB:4AJ3, ECO:0007744|PDB:4AJR, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI6 99) chain C residue 395 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI7 100) chain D residue 395 type BINDING sequence R description BINDING => ECO:0000269|PubMed:11284679, ECO:0000269|PubMed:2682654, ECO:0000269|PubMed:7761851, ECO:0007744|PDB:1AI2, ECO:0007744|PDB:9ICD source Swiss-Prot : SWS_FT_FI7 101) chain C residue 160 type SITE sequence Y description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8 102) chain C residue 230 type SITE sequence K description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8 103) chain D residue 160 type SITE sequence Y description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8 104) chain D residue 230 type SITE sequence K description Critical for catalysis => ECO:0000269|PubMed:7761851, ECO:0000269|PubMed:7819221 source Swiss-Prot : SWS_FT_FI8 105) chain C residue 303-322 type prosite sequence NLNGDYISDALAAQVGGIGI description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NLNGDYiSDalAaqv.GGIGI source prosite : PS00470 106) chain C residue 100 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9 107) chain C residue 242 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9 108) chain D residue 100 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9 109) chain D residue 242 type MOD_RES sequence K description N6-succinyllysine => ECO:0000269|PubMed:21151122 source Swiss-Prot : SWS_FT_FI9

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