eF-site ID 1f3m-ABCD
PDB Code 1f3m
Chain A, B, C, D

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Title CRYSTAL STRUCTURE OF HUMAN SERINE/THREONINE KINASE PAK1
Classification TRANSFERASE
Compound SERINE/THREONINE-PROTEIN KINASE PAK-ALPHA
Source Homo sapiens (Human) (PAK1_HUMAN)
Sequence A:  PSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQ
KKNPQAVLDVLEFYNSKKTSNSQKYMSFTD
B:  PSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQ
KKNPQAVLDVLEFYNSKKTSNSQKYMSFTD
C:  SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAM
DVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV
NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAA
VCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF
GFCAQITTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAI
EMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFR
DFLNRCLDMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIA
AAKEATK
D:  SDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAM
DVATGQEVAIRQMNLQQQPKKELIINEILVMRENKNPNIV
NYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAA
VCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDF
GFCAQITPGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEM
IEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDF
LNRCLDMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAA
KEATK
Description


Functional site

1) chain A
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE IOD A 601
source : AC1

2) chain C
residue 468
type
sequence N
description BINDING SITE FOR RESIDUE IOD C 602
source : AC2

3) chain C
residue 470
type
sequence L
description BINDING SITE FOR RESIDUE IOD C 602
source : AC2

4) chain D
residue 325
type
sequence P
description BINDING SITE FOR RESIDUE IOD D 604
source : AC4

5) chain A
residue 114
type
sequence K
description BINDING SITE FOR RESIDUE IOD A 607
source : AC6

6) chain A
residue 102
type
sequence Q
description BINDING SITE FOR RESIDUE IOD B 608
source : AC7

7) chain B
residue 98
type
sequence G
description BINDING SITE FOR RESIDUE IOD B 608
source : AC7

8) chain C
residue 466
type
sequence N
description BINDING SITE FOR RESIDUE IOD C 610
source : AC9

9) chain D
residue 268
type
sequence K
description BINDING SITE FOR RESIDUE IOD C 610
source : AC9

10) chain C
residue 364
type
sequence G
description BINDING SITE FOR RESIDUE IOD C 611
source : BC1

11) chain C
residue 325
type
sequence P
description BINDING SITE FOR RESIDUE IOD C 613
source : BC2

12) chain A
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE IOD A 614
source : BC3

13) chain A
residue 120
type
sequence N
description BINDING SITE FOR RESIDUE IOD B 615
source : BC4

14) chain B
residue 119
type
sequence K
description BINDING SITE FOR RESIDUE IOD B 615
source : BC4

15) chain D
residue 399
type
sequence M
description BINDING SITE FOR RESIDUE IOD D 619
source : BC7

16) chain A
residue 134
type
sequence K
description BINDING SITE FOR RESIDUE IOD A 620
source : BC8

17) chain D
residue 364
type
sequence G
description BINDING SITE FOR RESIDUE IOD D 621
source : BC9

18) chain D
residue 265
type
sequence D
description BINDING SITE FOR RESIDUE IOD D 622
source : CC1

19) chain C
residue 444
type
sequence K
description BINDING SITE FOR RESIDUE IOD C 623
source : CC2

20) chain C
residue 347
type
sequence L
description BINDING SITE FOR RESIDUE IOD D 625
source : CC4

21) chain D
residue 400
type
sequence D
description BINDING SITE FOR RESIDUE IOD D 625
source : CC4

22) chain C
residue 514
type
sequence E
description BINDING SITE FOR RESIDUE IOD C 627
source : CC5

23) chain D
residue 323
type
sequence K
description BINDING SITE FOR RESIDUE IOD D 628
source : CC6

24) chain D
residue 324
type
sequence N
description BINDING SITE FOR RESIDUE IOD D 628
source : CC6

25) chain C
residue 385-397
type prosite
sequence VIHRDIKSDNILL
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKsdNILL
source prosite : PS00108

26) chain C
residue 389
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI1

27) chain D
residue 389
type ACT_SITE
sequence D
description Proton acceptor => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 276
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

29) chain C
residue 299
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

30) chain C
residue 345
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

31) chain D
residue 276
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

32) chain D
residue 299
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

33) chain D
residue 345
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:22153498
source Swiss-Prot : SWS_FT_FI2

34) chain C
residue 285
type MOD_RES
sequence Y
description Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
source Swiss-Prot : SWS_FT_FI3

35) chain D
residue 285
type MOD_RES
sequence Y
description Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
source Swiss-Prot : SWS_FT_FI3

36) chain B
residue 131
type MOD_RES
sequence Y
description Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
source Swiss-Prot : SWS_FT_FI3

37) chain B
residue 142
type MOD_RES
sequence Y
description Phosphotyrosine; by JAK2 => ECO:0000269|PubMed:17726028, ECO:0000269|PubMed:17989089
source Swiss-Prot : SWS_FT_FI3

38) chain C
residue 423
type MOD_RES
sequence T
description Phosphothreonine; by autocatalysis, BRSK2 and PDPK1 => ECO:0000269|PubMed:10551809, ECO:0000269|PubMed:10995762, ECO:0000269|PubMed:22153498, ECO:0000269|PubMed:22669945
source Swiss-Prot : SWS_FT_FI4


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