eF-site ID 2c5v-ABCDFH
PDB Code 2c5v
Chain A, B, C, D, F, H

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Title Differential Binding Of Inhibitors To Active And Inactive Cdk2 Provides Insights For Drug Design
Classification CELL CYCLE
Compound CELL DIVISION PROTEIN KINASE 2
Source Homo sapiens (Human) (2C5V)
Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHL
B:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL
VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM
EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE
SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHL
D:  VPDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAIL
VDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQ
LVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRM
EHLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAM
FLGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPE
SLIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYK
NSKYHGVSLLNPPETLNL
F:  AAXRSLIXX
H:  AAXRSLIXX
Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.1.37), CYCLIN A2, ALA-ALA-ABA-ARG-SER-LEU-ILE-PFF-NH2


Functional site

1) chain A
residue 10
type
ligand
sequence I
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

2) chain A
residue 31
type
ligand
sequence A
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

3) chain A
residue 33
type
ligand
sequence K
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

4) chain A
residue 80
type
ligand
sequence F
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

5) chain A
residue 81
type
ligand
sequence E
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

6) chain A
residue 83
type
ligand
sequence L
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

7) chain A
residue 84
type
ligand
sequence H
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

8) chain A
residue 85
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

9) chain A
residue 86
type
ligand
sequence D
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

10) chain A
residue 89
type
ligand
sequence K
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

11) chain A
residue 134
type
ligand
sequence L
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

12) chain A
residue 145
type
ligand
sequence D
description BINDING SITE FOR RESIDUE CK4 A1297
source : AC1

13) chain C
residue 10
type
ligand
sequence I
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

14) chain C
residue 31
type
ligand
sequence A
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

15) chain C
residue 33
type
ligand
sequence K
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

16) chain C
residue 80
type
ligand
sequence F
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

17) chain C
residue 81
type
ligand
sequence E
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

18) chain C
residue 83
type
ligand
sequence L
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

19) chain C
residue 84
type
ligand
sequence H
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

20) chain C
residue 85
type
ligand
sequence Q
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

21) chain C
residue 86
type
ligand
sequence D
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

22) chain C
residue 89
type
ligand
sequence K
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

23) chain C
residue 134
type
ligand
sequence L
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

24) chain C
residue 145
type
ligand
sequence D
description BINDING SITE FOR RESIDUE CK4 C1297
source : AC2

25) chain A
residue 127
type ACT_SITE
ligand
sequence D
description Proton acceptor.
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 132
type METAL
ligand
sequence N
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI2

27) chain A
residue 145
type METAL
ligand
sequence D
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI2

28) chain A
residue 33
type BINDING
ligand
sequence K
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 86
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI3

30) chain A
residue 145
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI3

31) chain A
residue 9
type SITE
ligand
sequence K
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI4

32) chain A
residue 88-89
type SITE
ligand
sequence KK
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI4

33) chain A
residue 166
type SITE
ligand
sequence L
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI4

34) chain A
residue 10-18
type NP_BIND
ligand
sequence IGEGTYGVV
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI5

35) chain A
residue 81-83
type NP_BIND
ligand
sequence EFL
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI5

36) chain A
residue 129-132
type NP_BIND
ligand
sequence KPQN
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI5

37) chain C
residue 127
type ACT_SITE
ligand
sequence D
description Proton acceptor.
source Swiss-Prot : SWS_FT_FI6

38) chain C
residue 132
type METAL
ligand
sequence N
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI7

39) chain C
residue 145
type METAL
ligand
sequence D
description Magnesium. {ECO:0000269|PubMed:21565702}
source Swiss-Prot : SWS_FT_FI7

40) chain C
residue 33
type BINDING
ligand
sequence K
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

41) chain C
residue 86
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

42) chain C
residue 145
type BINDING
ligand
sequence D
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI8

43) chain C
residue 9
type SITE
ligand
sequence K
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

44) chain C
residue 88-89
type SITE
ligand
sequence KK
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

45) chain C
residue 166
type SITE
ligand
sequence L
description CDK7 binding.
source Swiss-Prot : SWS_FT_FI9

46) chain C
residue 10-18
type NP_BIND
ligand
sequence IGEGTYGVV
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

47) chain C
residue 81-83
type NP_BIND
ligand
sequence EFL
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

48) chain C
residue 129-132
type NP_BIND
ligand
sequence KPQN
description ATP. {ECO:0000255|PROSITE- ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702}.
source Swiss-Prot : SWS_FT_FI10

49) chain A
residue 149
type catalytic
ligand
sequence A
description Mapped from 2phk to 2c5v using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 98031892
source extCATRES : extCATRES1

50) chain A
residue 151
type catalytic
ligand
sequence A
description Mapped from 2phk to 2c5v using BLAST. All catalytic residues present. Original details record follows: a catalytic site defined by CATRES, Medline 98031892
source extCATRES : extCATRES1

51) 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

52) 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

53) 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

54) 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

55) 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

56) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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