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

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


Functional site

1) chain B
residue 252
type
sequence D
description binding site for residue MG A 501
source : AC1

2) chain B
residue 212
type
sequence K
description binding site for residue ICT A 502
source : AC2

3) chain B
residue 252
type
sequence D
description binding site for residue ICT A 502
source : AC2

4) chain B
residue 275
type
sequence D
description binding site for residue MG A 503
source : AC3

5) chain B
residue 77
type
sequence T
description binding site for residue ICT A 505
source : AC5

6) chain B
residue 94
type
sequence S
description binding site for residue ICT A 505
source : AC5

7) chain B
residue 96
type
sequence N
description binding site for residue ICT A 505
source : AC5

8) chain B
residue 100
type
sequence R
description binding site for residue ICT A 505
source : AC5

9) chain B
residue 109
type
sequence R
description binding site for residue ICT A 505
source : AC5

10) chain B
residue 132
type
sequence R
description binding site for residue ICT A 505
source : AC5

11) chain B
residue 139
type
sequence Y
description binding site for residue ICT A 505
source : AC5

12) chain B
residue 275
type
sequence D
description binding site for residue ICT A 505
source : AC5

13) chain B
residue 72
type
sequence K
description binding site for residue NAP B 501
source : AC6

14) chain B
residue 74
type
sequence A
description binding site for residue NAP B 501
source : AC6

15) chain B
residue 75
type
sequence T
description binding site for residue NAP B 501
source : AC6

16) chain B
residue 76
type
sequence I
description binding site for residue NAP B 501
source : AC6

17) chain B
residue 77
type
sequence T
description binding site for residue NAP B 501
source : AC6

18) chain B
residue 82
type
sequence R
description binding site for residue NAP B 501
source : AC6

19) chain B
residue 96
type
sequence N
description binding site for residue NAP B 501
source : AC6

20) chain B
residue 288
type
sequence L
description binding site for residue NAP B 501
source : AC6

21) chain B
residue 289
type
sequence G
description binding site for residue NAP B 501
source : AC6

22) chain B
residue 309
type
sequence H
description binding site for residue NAP B 501
source : AC6

23) chain B
residue 310
type
sequence G
description binding site for residue NAP B 501
source : AC6

24) chain B
residue 311
type
sequence T
description binding site for residue NAP B 501
source : AC6

25) chain B
residue 312
type
sequence V
description binding site for residue NAP B 501
source : AC6

26) chain B
residue 313
type
sequence T
description binding site for residue NAP B 501
source : AC6

27) chain B
residue 314
type
sequence R
description binding site for residue NAP B 501
source : AC6

28) chain B
residue 315
type
sequence H
description binding site for residue NAP B 501
source : AC6

29) chain B
residue 328
type
sequence N
description binding site for residue NAP B 501
source : AC6

30) chain B
residue 42
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI10

31) chain B
residue 81
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11

32) chain B
residue 224
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11

33) chain B
residue 233
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11

34) chain B
residue 243
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI11

35) chain B
residue 126
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI12

36) chain B
residue 400
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI12

37) chain B
residue 139
type SITE
sequence Y
description Critical for catalysis
source Swiss-Prot : SWS_FT_FI8

38) chain B
residue 212
type SITE
sequence K
description Critical for catalysis
source Swiss-Prot : SWS_FT_FI8

39) 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

40) 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

41) 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

42) chain B
residue 321
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI13

43) chain B
residue 389
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:O88844
source Swiss-Prot : SWS_FT_FI14

44) chain B
residue 212
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:15173171, ECO:0007744|PDB:1T0L
source Swiss-Prot : SWS_FT_FI4

45) 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

46) 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

47) 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

48) 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

49) 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

50) 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

51) 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

52) 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

53) 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


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