eF-site ID 6bl0-ABC PDB Code 6bl0 Chain A, B, C click to enlarge Title Novel Modes of Inhibition of Wild-Type IDH1:Direct Covalent Modification of His315 with Cmpd11 Classification OXIDOREDUCTASE/OXIDOREDUCTASE inhibitor Compound Isocitrate dehydrogenase [NADP] cytoplasmic Source (IDHC_HUMAN) Sequence A:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH B:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH C:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH Description Functional site 1) chain A residue 275 type sequence D description binding site for residue MG A 501 source : AC1 2) chain B residue 252 type sequence D description binding site for residue MG A 501 source : AC1 3) chain A residue 77 type sequence T description binding site for residue ICT A 502 source : AC2 4) chain A residue 94 type sequence S description binding site for residue ICT A 502 source : AC2 5) chain A residue 96 type sequence N description binding site for residue ICT A 502 source : AC2 6) chain A residue 100 type sequence R description binding site for residue ICT A 502 source : AC2 7) chain A residue 109 type sequence R description binding site for residue ICT A 502 source : AC2 8) chain A residue 132 type sequence R description binding site for residue ICT A 502 source : AC2 9) chain A residue 275 type sequence D description binding site for residue ICT A 502 source : AC2 10) chain B residue 212 type sequence K description binding site for residue ICT A 502 source : AC2 11) chain B residue 252 type sequence D description binding site for residue ICT A 502 source : AC2 12) chain A residue 252 type sequence D description binding site for residue MG A 503 source : AC3 13) chain B residue 275 type sequence D description binding site for residue MG A 503 source : AC3 14) chain A residue 289 type sequence G description binding site for residue DWJ A 504 source : AC4 15) chain A residue 309 type sequence H description binding site for residue DWJ A 504 source : AC4 16) chain A residue 312 type sequence V description binding site for residue DWJ A 504 source : AC4 17) chain A residue 314 type sequence R description binding site for residue DWJ A 504 source : AC4 18) chain A residue 315 type sequence H description binding site for residue DWJ A 504 source : AC4 19) chain A residue 318 type sequence M description binding site for residue DWJ A 504 source : AC4 20) chain A residue 324 type sequence E description binding site for residue DWJ A 504 source : AC4 21) chain A residue 325 type sequence T description binding site for residue DWJ A 504 source : AC4 22) chain A residue 326 type sequence S description binding site for residue DWJ A 504 source : AC4 23) chain A residue 327 type sequence T description binding site for residue DWJ A 504 source : AC4 24) chain A residue 328 type sequence N description binding site for residue DWJ A 504 source : AC4 25) chain A residue 374 type sequence K description binding site for residue DWJ A 504 source : AC4 26) chain A residue 212 type sequence K description binding site for residue ICT A 505 source : AC5 27) chain A residue 215 type sequence I description binding site for residue ICT A 505 source : AC5 28) chain A residue 252 type sequence D description binding site for residue ICT A 505 source : AC5 29) chain B residue 77 type sequence T description binding site for residue ICT A 505 source : AC5 30) chain B residue 94 type sequence S description binding site for residue ICT A 505 source : AC5 31) chain B residue 96 type sequence N description binding site for residue ICT A 505 source : AC5 32) chain B residue 100 type sequence R description binding site for residue ICT A 505 source : AC5 33) chain B residue 109 type sequence R description binding site for residue ICT A 505 source : AC5 34) chain B residue 132 type sequence R description binding site for residue ICT A 505 source : AC5 35) chain B residue 139 type sequence Y description binding site for residue ICT A 505 source : AC5 36) chain B residue 275 type sequence D description binding site for residue ICT A 505 source : AC5 37) chain A residue 250 type sequence L description binding site for residue NAP B 501 source : AC6 38) chain A residue 253 type sequence D description binding site for residue NAP B 501 source : AC6 39) chain A residue 257 type sequence Q description binding site for residue NAP B 501 source : AC6 40) chain A residue 260 type sequence K description binding site for residue NAP B 501 source : AC6 41) chain B residue 72 type sequence K description binding site for residue NAP B 501 source : AC6 42) chain B residue 74 type sequence A description binding site for residue NAP B 501 source : AC6 43) chain B residue 75 type sequence T description binding site for residue NAP B 501 source : AC6 44) chain B residue 76 type sequence I description binding site for residue NAP B 501 source : AC6 45) chain B residue 77 type sequence T description binding site for residue NAP B 501 source : AC6 46) chain B residue 82 type sequence R description binding site for residue NAP B 501 source : AC6 47) chain B residue 96 type sequence N description binding site for residue NAP B 501 source : AC6 48) chain B residue 288 type sequence L description binding site for residue NAP B 501 source : AC6 49) chain B residue 289 type sequence G description binding site for residue NAP B 501 source : AC6 50) chain B residue 309 type sequence H description binding site for residue NAP B 501 source : AC6 51) chain B residue 310 type sequence G description binding site for residue NAP B 501 source : AC6 52) chain B residue 311 type sequence T description binding site for residue NAP B 501 source : AC6 53) chain B residue 312 type sequence V description binding site for residue NAP B 501 source : AC6 54) chain B residue 313 type sequence T description binding site for residue NAP B 501 source : AC6 55) chain B residue 314 type sequence R description binding site for residue NAP B 501 source : AC6 56) chain B residue 315 type sequence H description binding site for residue NAP B 501 source : AC6 57) chain B residue 328 type sequence N description binding site for residue NAP B 501 source : AC6 58) chain C residue 252 type sequence D description binding site for residue MG C 500 source : AC7 59) chain C residue 275 type sequence D description binding site for residue MG C 500 source : AC7 60) chain C residue 77 type sequence T description binding site for residue ICT C 501 source : AC8 61) chain C residue 94 type sequence S description binding site for residue ICT C 501 source : AC8 62) chain C residue 96 type sequence N description binding site for residue ICT C 501 source : AC8 63) chain C residue 100 type sequence R description binding site for residue ICT C 501 source : AC8 64) chain C residue 109 type sequence R description binding site for residue ICT C 501 source : AC8 65) chain C residue 132 type sequence R description binding site for residue ICT C 501 source : AC8 66) chain C residue 139 type sequence Y description binding site for residue ICT C 501 source : AC8 67) chain C residue 212 type sequence K description binding site for residue ICT C 501 source : AC8 68) chain C residue 215 type sequence I description binding site for residue ICT C 501 source : AC8 69) chain C residue 252 type sequence D description binding site for residue ICT C 501 source : AC8 70) chain C residue 275 type sequence D description binding site for residue ICT C 501 source : AC8 71) chain C residue 72 type sequence K description binding site for residue NAP C 502 source : AC9 72) chain C residue 74 type sequence A description binding site for residue NAP C 502 source : AC9 73) chain C residue 75 type sequence T description binding site for residue NAP C 502 source : AC9 74) chain C residue 76 type sequence I description binding site for residue NAP C 502 source : AC9 75) chain C residue 77 type sequence T description binding site for residue NAP C 502 source : AC9 76) chain C residue 82 type sequence R description binding site for residue NAP C 502 source : AC9 77) chain C residue 96 type sequence N description binding site for residue NAP C 502 source : AC9 78) chain C residue 250 type sequence L description binding site for residue NAP C 502 source : AC9 79) chain C residue 253 type sequence D description binding site for residue NAP C 502 source : AC9 80) chain C residue 260 type sequence K description binding site for residue NAP C 502 source : AC9 81) chain C residue 288 type sequence L description binding site for residue NAP C 502 source : AC9 82) chain C residue 306 type sequence E description binding site for residue NAP C 502 source : AC9 83) chain C residue 307 type sequence A description binding site for residue NAP C 502 source : AC9 84) chain C residue 308 type sequence A description binding site for residue NAP C 502 source : AC9 85) chain C residue 309 type sequence H description binding site for residue NAP C 502 source : AC9 86) chain C residue 310 type sequence G description binding site for residue NAP C 502 source : AC9 87) chain C residue 311 type sequence T description binding site for residue NAP C 502 source : AC9 88) chain C residue 312 type sequence V description binding site for residue NAP C 502 source : AC9 89) chain C residue 313 type sequence T description binding site for residue NAP C 502 source : AC9 90) chain C residue 314 type sequence R description binding site for residue NAP C 502 source : AC9 91) chain C residue 315 type sequence H description binding site for residue NAP C 502 source : AC9 92) chain C residue 328 type sequence N description binding site for residue NAP C 502 source : AC9 93) chain A residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 94) chain B residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 95) chain C residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 96) chain A residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 97) chain C residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 98) chain C residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 99) chain C residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 100) chain A residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 101) chain A residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 102) chain A residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 103) chain B residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 104) chain B residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 105) chain B residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 106) chain B residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 107) chain C residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 108) chain A residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 109) chain A residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 110) chain B residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 111) chain B residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 112) chain C residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 113) chain C residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 114) chain A residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 115) chain A residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 116) chain B residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 117) chain B residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 118) chain C residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 119) chain C residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 120) chain A residue 75 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 121) chain A residue 310 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 122) chain A residue 328 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 123) chain B residue 75 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 124) chain B residue 310 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 125) chain B residue 328 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 126) chain C residue 75 type BINDING sequence T description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 127) chain C residue 310 type BINDING sequence G description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 128) chain C residue 328 type BINDING sequence N description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5L58, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI1 129) chain A residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 130) chain B residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 131) chain C residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 132) chain A residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 133) chain B residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 134) chain C residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 135) chain A residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 136) chain B residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 137) chain C residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 138) chain A residue 252 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI5 139) chain B residue 252 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI5 140) chain C residue 252 type BINDING sequence D description BINDING => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI5 141) chain A residue 260 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI6 142) chain B residue 260 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI6 143) chain C residue 260 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI6 144) chain A residue 275 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 145) chain A residue 279 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 146) chain B residue 275 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 147) chain B residue 279 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 148) chain C residue 275 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 149) chain C residue 279 type BINDING sequence D description in other chain => ECO:0000305|PubMed:15173171, ECO:0000305|PubMed:19935646, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM source Swiss-Prot : SWS_FT_FI7 150) chain A residue 77 type BINDING sequence T description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 151) chain C residue 94 type BINDING sequence S description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 152) chain C residue 109 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 153) chain C residue 132 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 154) chain A residue 94 type BINDING sequence S description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 155) chain A residue 109 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 156) chain A residue 132 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 157) chain B residue 77 type BINDING sequence T description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 158) chain B residue 94 type BINDING sequence S description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 159) chain B residue 109 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 160) chain B residue 132 type BINDING sequence R description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 161) chain C residue 77 type BINDING sequence T description in other chain => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI2 162) chain A residue 82 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI3 163) chain B residue 82 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI3 164) chain C residue 82 type BINDING sequence R description BINDING => ECO:0000269|PubMed:15173171, ECO:0000269|PubMed:19935646, ECO:0007744|PDB:1T09, ECO:0007744|PDB:1T0L, ECO:0007744|PDB:3INM, ECO:0007744|PDB:3MAP, ECO:0007744|PDB:3MAR, ECO:0007744|PDB:3MAS, ECO:0007744|PDB:4I3K, ECO:0007744|PDB:4I3L, ECO:0007744|PDB:4KZO, ECO:0007744|PDB:4L03, ECO:0007744|PDB:4L04, ECO:0007744|PDB:4L06, ECO:0007744|PDB:4UMX, ECO:0007744|PDB:4UMY, ECO:0007744|PDB:4XRX, ECO:0007744|PDB:4XS3, ECO:0007744|PDB:5DE1, ECO:0007744|PDB:5L57, ECO:0007744|PDB:5LGE, ECO:0007744|PDB:5SUN, ECO:0007744|PDB:5SVF, ECO:0007744|PDB:5TQH source Swiss-Prot : SWS_FT_FI3 165) chain A residue 271-290 type prosite sequence NYDGDVQSDSVAQGYGSLGM description IDH_IMDH Isocitrate and isopropylmalate dehydrogenases signature. NYDGDVqSDsvAqgy.GSLGM source prosite : PS00470

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