eF-site ID 6bky-C PDB Code 6bky Chain C 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 C:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSL Description Functional site 1) chain C residue 252 type sequence D description binding site for residue LMR D 501 source : AC1 2) chain C residue 252 type sequence D description binding site for residue MG D 502 source : AC2 3) chain C residue 121 type sequence V description binding site for residue K32 D 503 source : AC3 4) chain C residue 255 type sequence V description binding site for residue K32 D 503 source : AC3 5) chain C residue 259 type sequence M description binding site for residue K32 D 503 source : AC3 6) chain C residue 277 type sequence Q description binding site for residue K32 D 503 source : AC3 7) chain C residue 280 type sequence S description binding site for residue K32 D 503 source : AC3 8) chain C residue 275 type sequence D description binding site for residue MG D 504 source : AC4 9) chain C residue 279 type sequence D description binding site for residue MG D 504 source : AC4 10) 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 11) 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 12) 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 13) chain C residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 14) chain C residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 15) chain C residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 16) chain C residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 17) chain C residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 18) chain C residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 19) chain C residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 20) chain C residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 21) chain C residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 22) 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 23) 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 24) 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 25) 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 26) 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 27) chain C residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 28) 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 29) chain C residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 30) chain C residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 31) 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 32) 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 33) 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

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