eF-site ID 4z3v-A
PDB Code 4z3v
Chain A

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Title Fragment-Based Discovery of a Small Molecule Reversible Inhibitor of Bruton's Tyrosine Kinase
Classification TRANSFERASE
Compound Tyrosine-protein kinase BTK
Source Homo sapiens (Human) (BTK_HUMAN)
Sequence A:  GLGYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVA
IKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQR
PIFIITEYMANGCLLNYLREMRHRFQTQQLLEMCKDVCEA
MEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLD
DEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMW
EIYSLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYT
IMYSCWHEKADERPTFKILLSNILDVMDEES
Description


Functional site

1) chain A
residue 562
type
sequence R
description binding site for residue IMD A 701
source : AC1

2) chain A
residue 596
type
sequence M
description binding site for residue IMD A 701
source : AC1

3) chain A
residue 599
type
sequence E
description binding site for residue IMD A 701
source : AC1

4) chain A
residue 601
type
sequence F
description binding site for residue IMD A 701
source : AC1

5) chain A
residue 649
type
sequence S
description binding site for residue IMD A 701
source : AC1

6) chain A
residue 652
type
sequence L
description binding site for residue IMD A 701
source : AC1

7) chain A
residue 653
type
sequence D
description binding site for residue IMD A 701
source : AC1

8) chain A
residue 656
type
sequence D
description binding site for residue IMD A 701
source : AC1

9) chain A
residue 403
type
sequence T
description binding site for residue IPA A 703
source : AC3

10) chain A
residue 404
type
sequence F
description binding site for residue IPA A 703
source : AC3

11) chain A
residue 627
type
sequence Y
description binding site for residue IPA A 703
source : AC3

12) chain A
residue 495
type
sequence T
description binding site for residue EDO A 704
source : AC4

13) chain A
residue 496
type
sequence Q
description binding site for residue EDO A 704
source : AC4

14) chain A
residue 499
type
sequence L
description binding site for residue EDO A 704
source : AC4

15) chain A
residue 658
type
sequence E
description binding site for residue EDO A 704
source : AC4

16) chain A
residue 659
type
sequence S
description binding site for residue EDO A 704
source : AC4

17) chain A
residue 408
type
sequence L
description binding site for residue 4L6 A 705
source : AC5

18) chain A
residue 410
type
sequence T
description binding site for residue 4L6 A 705
source : AC5

19) chain A
residue 411
type
sequence G
description binding site for residue 4L6 A 705
source : AC5

20) chain A
residue 412
type
sequence Q
description binding site for residue 4L6 A 705
source : AC5

21) chain A
residue 413
type
sequence F
description binding site for residue 4L6 A 705
source : AC5

22) chain A
residue 414
type
sequence G
description binding site for residue 4L6 A 705
source : AC5

23) chain A
residue 416
type
sequence V
description binding site for residue 4L6 A 705
source : AC5

24) chain A
residue 428
type
sequence A
description binding site for residue 4L6 A 705
source : AC5

25) chain A
residue 474
type
sequence T
description binding site for residue 4L6 A 705
source : AC5

26) chain A
residue 475
type
sequence E
description binding site for residue 4L6 A 705
source : AC5

27) chain A
residue 477
type
sequence M
description binding site for residue 4L6 A 705
source : AC5

28) chain A
residue 528
type
sequence L
description binding site for residue 4L6 A 705
source : AC5

29) chain A
residue 539
type
sequence D
description binding site for residue 4L6 A 705
source : AC5

30) chain A
residue 625
type MOD_RES
sequence K
description Phosphoserine => ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI9

31) chain A
residue 570
type MOD_RES
sequence M
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI6

32) chain A
residue 583
type MOD_RES
sequence F
description Phosphotyrosine => ECO:0000269|PubMed:15375214
source Swiss-Prot : SWS_FT_FI7

33) chain A
residue 589
type MOD_RES
sequence E
description Phosphoserine => ECO:0000269|PubMed:15375214
source Swiss-Prot : SWS_FT_FI8

34) chain A
residue 396
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

35) chain A
residue 440
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:20052711, ECO:0007744|PDB:3K54, ECO:0007744|PDB:3OCT
source Swiss-Prot : SWS_FT_FI3

36) chain A
residue 487
type ACT_SITE
sequence R
description Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
source Swiss-Prot : SWS_FT_FI1

37) chain A
residue 408-430
type prosite
sequence LGTGQFGVVKYGKWRGQYDVAIK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGQFGVVKyGkwrgqyd...........VAIK
source prosite : PS00107

38) chain A
residue 517-529
type prosite
sequence FLHRDLAARNCLV
description PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FLHrDLAARNCLV
source prosite : PS00109

39) chain A
residue 508
type BINDING
sequence A
description BINDING => ECO:0000269|PubMed:21280133, ECO:0007744|PDB:3PIY
source Swiss-Prot : SWS_FT_FI4

40) chain A
residue 517
type MOD_RES
sequence F
description Phosphotyrosine; by LYN and SYK => ECO:0000269|PubMed:8630736, ECO:0000269|PubMed:9012831
source Swiss-Prot : SWS_FT_FI5


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