eF-site ID 2f6j-ABCP
PDB Code 2f6j
Chain A, B, C, P

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Title Crystal structure of PHD finger-linker-bromodomain fragment of human BPTF in the H3(1-15)K4me3 bound state
Classification TRANSCRIPTION
Compound bromodomain PHD finger transcription factor
Source (2F6J)
Sequence A:  DTKLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEA
ELIDEYVCPQCQSTEDAXTVLTPLTEKDYEGLKRVLRSLQ
AHKXAWPFLEPVDPNDAPDYYGVIKEPXDLATXEERVQRR
YYEKLTEFVADXTKIFDNCRYYNPSDSPFYQCAEVLESFF
VQKLKGFK
B:  TKLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAE
LIDEYVCPQCQSTEDAXTVLTPLTEKDYEGLKRVLRSLQA
HKXAWPFLEPVDPNDAPDYYGVIKEPXDLATXEERVQRRY
YEKLTEFVADXTKIFDNCRYYNPSDSPFYQCAEVLESFFV
QKLKGFK
C:  KLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAEL
IDEYVCPQCQSTEDAXTVLTPLTEKDYEGLKRVLRSLQAH
KXAWPFLEPVDPNDAPDYYGVIKEPXDLATXEERVQRRYY
EKLTEFVADXTKIFDNCRYYNPSDSPFYQCAEVLESFFVQ
KLKGFK
P:  ARTXQT
Description (1)  bromodomain PHD finger transcription factor/histone H3 tail (1-15)K4me3


Functional site

1) chain A
residue 11
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

2) chain A
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

3) chain A
residue 34
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

4) chain A
residue 37
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1001
source : AC1

5) chain A
residue 26
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1002
source : AC2

6) chain A
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1002
source : AC2

7) chain A
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1002
source : AC2

8) chain A
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1002
source : AC2

9) chain B
residue 11
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1003
source : AC3

10) chain B
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1003
source : AC3

11) chain B
residue 34
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1003
source : AC3

12) chain B
residue 37
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1003
source : AC3

13) chain B
residue 26
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1004
source : AC4

14) chain B
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1004
source : AC4

15) chain B
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1004
source : AC4

16) chain B
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1004
source : AC4

17) chain C
residue 11
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1005
source : AC5

18) chain C
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1005
source : AC5

19) chain C
residue 34
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 1005
source : AC5

20) chain C
residue 37
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1005
source : AC5

21) chain C
residue 26
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1006
source : AC6

22) chain C
residue 29
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1006
source : AC6

23) chain C
residue 53
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1006
source : AC6

24) chain C
residue 56
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 1006
source : AC6

25) chain A
residue 90-147
type prosite
sequence AWPFLEPVDPNDAPDYYGVIKEPXDLATXEERVQRRYYEK
LTEFVADXTKIFDNCRYY
description BROMODOMAIN_1 Bromodomain signature. AwpFlepvDpndap..DYYgvIkepMdlatMeervqrry..Yekltefvadmtk.IfdNCryY
source prosite : PS00633

26) chain A
residue 11-26
type prosite
sequence CICKTPYDESKFYIGC
description EGF_2 EGF-like domain signature 2. CiCktPYdeskfyigC
source prosite : PS01186

27) chain A
residue 11-56
type prosite
sequence CICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAELIDE
YVCPQC
description ZF_PHD_1 Zinc finger PHD-type signature. Ci.Cktpydeskfy...................................IgCdr..Cqnw.YHgrCvgilqseaelide................................YvCpqC
source prosite : PS01359

28) chain A
residue 10
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

29) chain C
residue 17
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

30) chain C
residue 23
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

31) chain C
residue 32
type SITE
sequence W
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

32) chain A
residue 17
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

33) chain A
residue 23
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

34) chain A
residue 32
type SITE
sequence W
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

35) chain B
residue 10
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

36) chain B
residue 17
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

37) chain B
residue 23
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

38) chain B
residue 32
type SITE
sequence W
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 10
type SITE
sequence Y
description Histone H3K4me3 binding
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 8-59
type ZN_FING
sequence KLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAEL
IDEYVCPQCQST
description PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
source Swiss-Prot : SWS_FT_FI1

41) chain B
residue 8-59
type ZN_FING
sequence KLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAEL
IDEYVCPQCQST
description PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
source Swiss-Prot : SWS_FT_FI1

42) chain C
residue 8-59
type ZN_FING
sequence KLYCICKTPYDESKFYIGCDRCQNWYHGRCVGILQSEAEL
IDEYVCPQCQST
description PHD-type 2 => ECO:0000255|PROSITE-ProRule:PRU00146
source Swiss-Prot : SWS_FT_FI1


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