eF-site ID 6bky-B PDB Code 6bky Chain B click to enlarge Title Novel Binding Modes of Inhibition of Wild-Type IDH1: Allosteric Inhibition with Cmpd2 Classification OXIDOREDUCTASE/OXIDOREDUCTASE inhibitor Compound Isocitrate dehydrogenase [NADP] cytoplasmic Source (IDHC_HUMAN) Sequence B:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLS Description Functional site 1) chain B residue 275 type sequence D description binding site for residue MG A 501 source : AC7 2) chain B residue 279 type sequence D description binding site for residue MG A 501 source : AC7 3) chain B residue 121 type sequence V description binding site for residue K32 A 502 source : AC8 4) chain B residue 255 type sequence V description binding site for residue K32 A 502 source : AC8 5) chain B residue 259 type sequence M description binding site for residue K32 A 502 source : AC8 6) chain B residue 277 type sequence Q description binding site for residue K32 A 502 source : AC8 7) chain B residue 280 type sequence S description binding site for residue K32 A 502 source : AC8 8) chain B residue 77 type sequence T description binding site for residue LMR A 503 source : AC9 9) chain B residue 94 type sequence S description binding site for residue LMR A 503 source : AC9 10) chain B residue 96 type sequence N description binding site for residue LMR A 503 source : AC9 11) chain B residue 100 type sequence R description binding site for residue LMR A 503 source : AC9 12) chain B residue 109 type sequence R description binding site for residue LMR A 503 source : AC9 13) chain B residue 132 type sequence R description binding site for residue LMR A 503 source : AC9 14) chain B residue 139 type sequence Y description binding site for residue LMR A 503 source : AC9 15) chain B residue 275 type sequence D description binding site for residue LMR A 503 source : AC9 16) 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 17) 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 18) 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 19) chain B residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 20) chain B residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 21) chain B residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 22) chain B residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 23) chain B residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 24) chain B residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 25) chain B residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 26) chain B residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 27) chain B residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 28) 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 29) 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 30) 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 31) 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 32) 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 33) chain B residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 34) 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 35) chain B residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 36) chain B residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 37) 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 38) 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 39) 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

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