eF-site ID 6bl0-C
PDB Code 6bl0
Chain C

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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 C:  KKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSY
DLGIENRDATNDQVTKDAAEAIKKHNVGVKCATITPDEKR
VEEFKLKQMWKSPNGTIRNILGGTVFREAIICKNIPRLVS
GWVKPIIIGRHAYGDQYRATDFVVPGPGKVEITYTPSDGT
QKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMALS
KGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQ
KIWYEHRLIDDMVAQAMKSEGGFIWACKNYDGDVQSDSVA
QGYGSLGMMTSVLVCPDGKTVEAEAAHGTVTRHYRMYQKG
QETSTNPIASIFAWTRGLAHRAKLDNNKELAFFANALEEV
SIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDKLG
ENLKIKLAQAKLSLEH
Description


Functional site
1) chain C
residue 252
type
sequence D
description binding site for residue MG C 500
source : AC7
2) chain C
residue 275
type
sequence D
description binding site for residue MG C 500
source : AC7
3) chain C
residue 77
type
sequence T
description binding site for residue ICT C 501
source : AC8
4) chain C
residue 94
type
sequence S
description binding site for residue ICT C 501
source : AC8
5) chain C
residue 96
type
sequence N
description binding site for residue ICT C 501
source : AC8
6) chain C
residue 100
type
sequence R
description binding site for residue ICT C 501
source : AC8
7) chain C
residue 109
type
sequence R
description binding site for residue ICT C 501
source : AC8
8) chain C
residue 132
type
sequence R
description binding site for residue ICT C 501
source : AC8
9) chain C
residue 139
type
sequence Y
description binding site for residue ICT C 501
source : AC8
10) chain C
residue 212
type
sequence K
description binding site for residue ICT C 501
source : AC8
11) chain C
residue 215
type
sequence I
description binding site for residue ICT C 501
source : AC8
12) chain C
residue 252
type
sequence D
description binding site for residue ICT C 501
source : AC8
13) chain C
residue 275
type
sequence D
description binding site for residue ICT C 501
source : AC8
14) chain C
residue 72
type
sequence K
description binding site for residue NAP C 502
source : AC9
15) chain C
residue 74
type
sequence A
description binding site for residue NAP C 502
source : AC9
16) chain C
residue 75
type
sequence T
description binding site for residue NAP C 502
source : AC9
17) chain C
residue 76
type
sequence I
description binding site for residue NAP C 502
source : AC9
18) chain C
residue 77
type
sequence T
description binding site for residue NAP C 502
source : AC9
19) chain C
residue 82
type
sequence R
description binding site for residue NAP C 502
source : AC9
20) chain C
residue 96
type
sequence N
description binding site for residue NAP C 502
source : AC9
21) chain C
residue 250
type
sequence L
description binding site for residue NAP C 502
source : AC9
22) chain C
residue 253
type
sequence D
description binding site for residue NAP C 502
source : AC9
23) chain C
residue 260
type
sequence K
description binding site for residue NAP C 502
source : AC9
24) chain C
residue 288
type
sequence L
description binding site for residue NAP C 502
source : AC9
25) chain C
residue 306
type
sequence E
description binding site for residue NAP C 502
source : AC9
26) chain C
residue 307
type
sequence A
description binding site for residue NAP C 502
source : AC9
27) chain C
residue 308
type
sequence A
description binding site for residue NAP C 502
source : AC9
28) chain C
residue 309
type
sequence H
description binding site for residue NAP C 502
source : AC9
29) chain C
residue 310
type
sequence G
description binding site for residue NAP C 502
source : AC9
30) chain C
residue 311
type
sequence T
description binding site for residue NAP C 502
source : AC9
31) chain C
residue 312
type
sequence V
description binding site for residue NAP C 502
source : AC9
32) chain C
residue 313
type
sequence T
description binding site for residue NAP C 502
source : AC9
33) chain C
residue 314
type
sequence R
description binding site for residue NAP C 502
source : AC9
34) chain C
residue 315
type
sequence H
description binding site for residue NAP C 502
source : AC9
35) chain C
residue 328
type
sequence N
description binding site for residue NAP C 502
source : AC9
36) 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
37) 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
38) 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
39) chain C
residue 42
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10
40) chain C
residue 224
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11
41) chain C
residue 233
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11
42) chain C
residue 243
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11
43) chain C
residue 81
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11
44) chain C
residue 126
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI12
45) chain C
residue 400
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI12
46) chain C
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI13
47) chain C
residue 389
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI14
48) 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
49) 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
50) 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
51) 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
52) 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
53) chain C
residue 212
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
source Swiss-Prot : SWS_FT_FI4
54) 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
55) 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
56) 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
57) 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
58) chain C
residue 139
type SITE
sequence Y
description Critical for catalysis
source Swiss-Prot : SWS_FT_FI8
59) chain C
residue 212
type SITE
sequence K
description Critical for catalysis
source Swiss-Prot : SWS_FT_FI8

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