eF-site ID 1oi9-ABCD
PDB Code 1oi9
Chain A, B, C, D

click to enlarge
Title Structure of human Thr160-phospho CDK2/cyclin A complexed with a 6-cyclohexylmethyloxy-2-anilino-purine inhibitor
Classification KINASE
Compound CELL DIVISION PROTEIN KINASE 2
Source Homo sapiens (Human) (CGA2_HUMAN)
Sequence A:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYX
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHL
B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL
VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM
EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE
SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT
ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV
FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH
SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY
XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR
RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS
FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA
ALAHPFFQDVTKPVPHL
D:  YHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILVDW
LVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVG
TAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHL
VLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMFLG
ELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPESLI
RKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKNSK
YHGVSLLNPPETL
Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.1.37), CYCLIN A2


Functional site

1) chain B
residue 200
type
ligand
sequence M
description BINDING SITE FOR RESIDUE MG B1433
source : AC1

2) chain B
residue 203
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE MG B1433
source : AC1

3) chain B
residue 206
type
ligand
sequence I
description BINDING SITE FOR RESIDUE MG B1433
source : AC1

4) chain A
residue 10
type
ligand
sequence I
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

5) chain A
residue 12
type
ligand
sequence E
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

6) chain A
residue 31
type
ligand
sequence A
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

7) chain A
residue 64
type
ligand
sequence V
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

8) chain A
residue 80
type
ligand
sequence F
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

9) chain A
residue 81
type
ligand
sequence E
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

10) chain A
residue 83
type
ligand
sequence L
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

11) chain A
residue 84
type
ligand
sequence H
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

12) chain A
residue 85
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

13) chain A
residue 86
type
ligand
sequence D
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

14) chain A
residue 132
type
ligand
sequence N
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

15) chain A
residue 134
type
ligand
sequence L
description BINDING SITE FOR RESIDUE N20 A1298
source : AC2

16) chain C
residue 12
type
ligand
sequence E
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

17) chain C
residue 31
type
ligand
sequence A
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

18) chain C
residue 64
type
ligand
sequence V
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

19) chain C
residue 80
type
ligand
sequence F
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

20) chain C
residue 81
type
ligand
sequence E
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

21) chain C
residue 82
type
ligand
sequence F
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

22) chain C
residue 83
type
ligand
sequence L
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

23) chain C
residue 84
type
ligand
sequence H
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

24) chain C
residue 85
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

25) chain C
residue 86
type
ligand
sequence D
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

26) chain C
residue 89
type
ligand
sequence K
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

27) chain C
residue 132
type
ligand
sequence N
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

28) chain C
residue 134
type
ligand
sequence L
description BINDING SITE FOR RESIDUE N20 C1298
source : AC3

29) chain B
residue 189
type
ligand
sequence M
description BINDING SITE FOR RESIDUE SGM B1193
source : AC4

30) chain B
residue 193
type
ligand
sequence C
description BINDING SITE FOR RESIDUE SGM B1193
source : AC4

31) chain B
residue 241
type
ligand
sequence R
description BINDING SITE FOR RESIDUE SGM B1193
source : AC4

32) chain B
residue 305
type
ligand
sequence D
description BINDING SITE FOR RESIDUE SGM B1193
source : AC4

33) chain D
residue 189
type
ligand
sequence M
description BINDING SITE FOR RESIDUE SGM D1193
source : AC5

34) chain D
residue 192
type
ligand
sequence K
description BINDING SITE FOR RESIDUE SGM D1193
source : AC5

35) chain D
residue 193
type
ligand
sequence C
description BINDING SITE FOR RESIDUE SGM D1193
source : AC5

36) chain D
residue 241
type
ligand
sequence R
description BINDING SITE FOR RESIDUE SGM D1193
source : AC5

37) chain D
residue 305
type
ligand
sequence D
description BINDING SITE FOR RESIDUE SGM D1193
source : AC5

38) chain A
residue 131
type ACT_SITE
ligand
sequence Q
description Proton acceptor.
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 37
type BINDING
ligand
sequence L
description ATP.
source Swiss-Prot : SWS_FT_FI2

40) chain A
residue 90
type BINDING
ligand
sequence F
description ATP.
source Swiss-Prot : SWS_FT_FI2

41) chain A
residue 149
type BINDING
ligand
sequence A
description ATP.
source Swiss-Prot : SWS_FT_FI2

42) chain A
residue 14-22
type NP_BIND
ligand
sequence TYGVVYKAR
description ATP.
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 85-87
type NP_BIND
ligand
sequence QDL
description ATP.
source Swiss-Prot : SWS_FT_FI3

44) chain A
residue 133-136
type NP_BIND
ligand
sequence LLIN
description ATP.
source Swiss-Prot : SWS_FT_FI3

45) chain C
residue 131
type ACT_SITE
ligand
sequence Q
description Proton acceptor.
source Swiss-Prot : SWS_FT_FI4

46) chain C
residue 37
type BINDING
ligand
sequence L
description ATP.
source Swiss-Prot : SWS_FT_FI5

47) chain C
residue 90
type BINDING
ligand
sequence F
description ATP.
source Swiss-Prot : SWS_FT_FI5

48) chain C
residue 149
type BINDING
ligand
sequence A
description ATP.
source Swiss-Prot : SWS_FT_FI5

49) chain C
residue 14-22
type NP_BIND
ligand
sequence TYGVVYKAR
description ATP.
source Swiss-Prot : SWS_FT_FI6

50) chain C
residue 85-87
type NP_BIND
ligand
sequence QDL
description ATP.
source Swiss-Prot : SWS_FT_FI6

51) chain C
residue 133-136
type NP_BIND
ligand
sequence LLIN
description ATP.
source Swiss-Prot : SWS_FT_FI6

52) chain A
residue 149
type catalytic
ligand
sequence A
description Mapped from 2phk to 1oi9 using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 98031892
source extCATRES : extCATRES1

53) chain A
residue 151
type catalytic
ligand
sequence A
description Mapped from 2phk to 1oi9 using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 98031892
source extCATRES : extCATRES1

54) chain A
residue 10-33
type prosite
ligand
sequence IGEGTYGVVYKARNKLTGEVVALK
description Protein kinases ATP-binding region signature.[LIV]-G-{P}-G-{P}-[FYWMGSTNH]-[SGA]-{PW}-[LIVCAT]-{PD}-x-[GSTACLIVMFY]-x(5,18)-[LIVMFYWCSTAR]-[AIVP]-[LIVMFAGCKR]-K.
source prosite : PS00107

55) chain C
residue 10-33
type prosite
ligand
sequence IGEGTYGVVYKARNKLTGEVVALK
description Protein kinases ATP-binding region signature.[LIV]-G-{P}-G-{P}-[FYWMGSTNH]-[SGA]-{PW}-[LIVCAT]-{PD}-x-[GSTACLIVMFY]-x(5,18)-[LIVMFYWCSTAR]-[AIVP]-[LIVMFAGCKR]-K.
source prosite : PS00107

56) chain A
residue 123-135
type prosite
ligand
sequence VLHRDLKPQNLLI
description Serine/Threonine protein kinases active-site signature.[LIVMFYC]-x-[HY]-x-D-[LIVMFY]-K-x(2)-N-[LIVMFYCT](3).
source prosite : PS00108

57) chain C
residue 123-135
type prosite
ligand
sequence VLHRDLKPQNLLI
description Serine/Threonine protein kinases active-site signature.[LIVMFYC]-x-[HY]-x-D-[LIVMFY]-K-x(2)-N-[LIVMFYCT](3).
source prosite : PS00108

58) chain B
residue 211-242
type prosite
ligand
sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF
description Cyclins signature.R-x(2)-[LIVMSA]-x(2)-[FYWS]-[LIVM]-x(8)-[LIVMFC]-x(4)-[LIVMFYA]-x(2)-[STAGC]-[LIVMFYQ]-x-[LIVMFYC]-[LIVMFY]-D-[RKH]-[LIVMFYW].
source prosite : PS00292

59) chain D
residue 211-242
type prosite
ligand
sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF
description Cyclins signature.R-x(2)-[LIVMSA]-x(2)-[FYWS]-[LIVM]-x(8)-[LIVMFC]-x(4)-[LIVMFYA]-x(2)-[STAGC]-[LIVMFYQ]-x-[LIVMFYC]-[LIVMFY]-D-[RKH]-[LIVMFYW].
source prosite : PS00292

60) chain A
residue 131
type catalytic
ligand
sequence Q
description Annotated By Reference To The Literature 1ir3
source CSA : CSA1

61) chain A
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA1

62) chain C
residue 131
type catalytic
ligand
sequence Q
description Annotated By Reference To The Literature 1ir3
source CSA : CSA2

63) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA2

64) chain A
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA3

65) chain A
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA3

66) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA4

67) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA4

68) chain A
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA5

69) chain A
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA5

70) chain A
residue 165
type catalytic
ligand
sequence T
description Annotated By Reference To The Literature 1ir3
source CSA : CSA5

71) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

72) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

73) chain C
residue 165
type catalytic
ligand
sequence T
description Annotated By Reference To The Literature 1ir3
source CSA : CSA6

74) chain A
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA7

75) chain A
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA7

76) chain A
residue 132
type catalytic
ligand
sequence N
description Annotated By Reference To The Literature 1ir3
source CSA : CSA7

77) chain C
residue 127
type catalytic
ligand
sequence D
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8

78) chain C
residue 129
type catalytic
ligand
sequence K
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8

79) chain C
residue 132
type catalytic
ligand
sequence N
description Annotated By Reference To The Literature 1ir3
source CSA : CSA8


Display surface

Download
Links