eF-site ID 3e8d-ABCD
PDB Code 3e8d
Chain A, B, C, D

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Title Crystal structures of the kinase domain of AKT2 in complex with ATP-competitive inhibitors
Classification TRANSFERASE
Compound RAC-beta serine/threonine-protein kinase
Source Homo sapiens (Human) (GSK3B_HUMAN)
Sequence A:  KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRK
EVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRL
CFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY
LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGA
TMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL
KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPP
FKPQVTSEVDTRYFDDEFTAQSITHFPQFDYSASIR
B:  KVTMNDFDYLKLLGKGTFGKVILVREKATGRYYAMKILRK
EVIIAKDEVAHTVTESRVLQNTRHPFLTALKYAFQTHDRL
CFVMEYANGGELFFHLSRERVFTEERARFYGAEIVSALEY
LHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGISDGA
TMKXFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC
GRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLL
KKDPKQRLGGGPSDAKEVMEHRFFLSINWQDVVQKKLLPP
FKPQVTSEVDTRYFDDEFTAQSIQRTHFPQFDYSASIR
C:  GRPRTTSFAE
D:  GRPRTTSFAE
Description


Functional site

1) chain A
residue 160
type
sequence K
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

2) chain A
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

3) chain A
residue 164
type
sequence G
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

4) chain A
residue 165
type
sequence K
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

5) chain A
residue 166
type
sequence V
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

6) chain A
residue 179
type
sequence A
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

7) chain A
residue 181
type
sequence K
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

8) chain A
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

9) chain A
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

10) chain A
residue 227
type
sequence F
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

11) chain A
residue 229
type
sequence M
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

12) chain A
residue 230
type
sequence E
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

13) chain A
residue 231
type
sequence Y
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

14) chain A
residue 232
type
sequence A
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

15) chain A
residue 280
type
sequence N
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

16) chain A
residue 282
type
sequence M
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

17) chain A
residue 292
type
sequence T
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

18) chain A
residue 293
type
sequence D
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

19) chain A
residue 294
type
sequence F
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

20) chain A
residue 439
type
sequence F
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

21) chain C
residue 9
type
sequence S
description BINDING SITE FOR RESIDUE G98 A 1
source : AC1

22) chain B
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

23) chain B
residue 164
type
sequence G
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

24) chain B
residue 166
type
sequence V
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

25) chain B
residue 179
type
sequence A
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

26) chain B
residue 181
type
sequence K
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

27) chain B
residue 200
type
sequence E
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

28) chain B
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

29) chain B
residue 227
type
sequence F
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

30) chain B
residue 229
type
sequence M
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

31) chain B
residue 230
type
sequence E
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

32) chain B
residue 231
type
sequence Y
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

33) chain B
residue 232
type
sequence A
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

34) chain B
residue 280
type
sequence N
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

35) chain B
residue 282
type
sequence M
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

36) chain B
residue 292
type
sequence T
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

37) chain B
residue 293
type
sequence D
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

38) chain B
residue 294
type
sequence F
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

39) chain B
residue 439
type
sequence F
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

40) chain D
residue 9
type
sequence S
description BINDING SITE FOR RESIDUE G98 B 1
source : AC2

41) chain C
residue 9
type MOD_RES
sequence S
description Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 => ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:8250835
source Swiss-Prot : SWS_FT_FI1

42) chain D
residue 9
type MOD_RES
sequence S
description Phosphoserine; by PKB/AKT1, RPS6KA3 and SGK3 => ECO:0000269|PubMed:12054501, ECO:0000269|PubMed:16484495, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:25169422, ECO:0000269|PubMed:8250835
source Swiss-Prot : SWS_FT_FI1

43) chain A
residue 280
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12434148
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 293
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12434148
source Swiss-Prot : SWS_FT_FI3

45) chain B
residue 280
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:12434148
source Swiss-Prot : SWS_FT_FI3

46) chain B
residue 293
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:12434148
source Swiss-Prot : SWS_FT_FI3

47) chain A
residue 474
type MOD_RES
sequence D
description Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI7

48) chain B
residue 474
type MOD_RES
sequence D
description Phosphoserine => ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI7

49) chain A
residue 158-191
type prosite
sequence LGKGTFGKVILVREKATGRYYAMKILRKEVIIAK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGTFGKVIlVrekatgryyamkilrkevIIAK
source prosite : PS00107

50) chain A
residue 271-283
type prosite
sequence VVYRDIKLENLML
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDIKleNLML
source prosite : PS00108

51) chain A
residue 306
type CARBOHYD
sequence T
description O-linked (GlcNAc) threonine => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

52) chain A
residue 313
type CARBOHYD
sequence T
description O-linked (GlcNAc) threonine => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

53) chain B
residue 306
type CARBOHYD
sequence T
description O-linked (GlcNAc) threonine => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

54) chain B
residue 313
type CARBOHYD
sequence T
description O-linked (GlcNAc) threonine => ECO:0000250
source Swiss-Prot : SWS_FT_FI8

55) chain A
residue 158
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

56) chain A
residue 181
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

57) chain B
residue 158
type BINDING
sequence L
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

58) chain B
residue 181
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
source Swiss-Prot : SWS_FT_FI2

59) chain A
residue 309
type MOD_RES
sequence X
description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493
source Swiss-Prot : SWS_FT_FI4

60) chain B
residue 309
type MOD_RES
sequence X
description Phosphothreonine; by PDPK1 => ECO:0000269|PubMed:12434148, ECO:0000269|PubMed:15890450, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:9512493
source Swiss-Prot : SWS_FT_FI4

61) chain A
residue 447
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI5

62) chain A
residue 478
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI5

63) chain B
residue 447
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI5

64) chain B
residue 478
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI5


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