eF-site ID 6bky-A PDB Code 6bky Chain A 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 A:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG ENLKIKLAQAKLSLEH Description Functional site 1) chain A residue 252 type sequence D description binding site for residue MG A 501 source : AC7 2) chain A residue 121 type sequence V description binding site for residue K32 A 502 source : AC8 3) chain A residue 255 type sequence V description binding site for residue K32 A 502 source : AC8 4) chain A residue 259 type sequence M description binding site for residue K32 A 502 source : AC8 5) chain A residue 277 type sequence Q description binding site for residue K32 A 502 source : AC8 6) chain A residue 280 type sequence S description binding site for residue K32 A 502 source : AC8 7) chain A residue 252 type sequence D description binding site for residue LMR A 503 source : AC9 8) 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 9) 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 10) 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 11) chain A residue 42 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI10 12) chain A residue 81 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 13) chain A residue 224 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 14) chain A residue 233 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 15) chain A residue 243 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI11 16) chain A residue 126 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 17) chain A residue 400 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI12 18) chain A residue 321 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI13 19) chain A residue 389 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:O88844 source Swiss-Prot : SWS_FT_FI14 20) 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 21) 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 22) 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 23) 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 24) 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 25) chain A residue 212 type BINDING sequence K description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L source Swiss-Prot : SWS_FT_FI4 26) 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 27) 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 28) 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 29) 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 30) chain A residue 139 type SITE sequence Y description Critical for catalysis source Swiss-Prot : SWS_FT_FI8 31) chain A residue 212 type SITE sequence K description Critical for catalysis source Swiss-Prot : SWS_FT_FI8

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