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

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Title Cdk2/CyclinA complexed with a imidazo triazin-2-amine
Classification TRANSFERASE/CELL CYCLE
Compound Cell division protein kinase 2
Source (CCNA2_HUMAN)
Sequence A:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLTEG
VPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL
HQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRV
LHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEV
VTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALF
PGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKW
ARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAH
PFFQDVTKPVPHLRL
B:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV
DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL
VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME
HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF
LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES
LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN
SKYHGVSLLNPPETLNL
C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLTEG
VPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFL
HQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRV
LHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEV
VTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALF
PGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKW
ARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAH
PFFQDVTKPVPHL
D:  PDYHEDIHTYLREMEVKCKPKVGYMKKQPDITNSMRAILV
DWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQL
VGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRME
HLVLKVLTFDLAAPTVNQFLTQYFLHQQPANCKVESLAMF
LGELSLIDADPYLKYLPSVIAGAAFHLALYTVTGQSWPES
LIRKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKN
SKYHGVSLLNPPETLNL
Description


Functional site

1) chain A
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

2) chain A
residue 11
type
sequence G
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

3) chain A
residue 12
type
sequence E
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

4) chain A
residue 18
type
sequence V
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

5) chain A
residue 31
type
sequence A
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

6) chain A
residue 80
type
sequence F
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

7) chain A
residue 81
type
sequence E
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

8) chain A
residue 82
type
sequence F
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

9) chain A
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

10) chain A
residue 84
type
sequence H
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

11) chain A
residue 85
type
sequence Q
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

12) chain A
residue 86
type
sequence D
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

13) chain A
residue 89
type
sequence K
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

14) chain A
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE T2A A 501
source : AC1

15) chain C
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

16) chain C
residue 31
type
sequence A
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

17) chain C
residue 64
type
sequence V
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

18) chain C
residue 80
type
sequence F
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

19) chain C
residue 81
type
sequence E
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

20) chain C
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

21) chain C
residue 84
type
sequence H
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

22) chain C
residue 86
type
sequence D
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

23) chain C
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE T2A C 501
source : AC2

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

25) chain A
residue 88
type SITE
sequence K
description CDK7 binding
source Swiss-Prot : SWS_FT_FI4

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

27) chain C
residue 9
type SITE
sequence K
description CDK7 binding
source Swiss-Prot : SWS_FT_FI4

28) chain C
residue 88
type SITE
sequence K
description CDK7 binding
source Swiss-Prot : SWS_FT_FI4

29) chain C
residue 166
type SITE
sequence L
description CDK7 binding
source Swiss-Prot : SWS_FT_FI4

30) chain A
residue 15
type MOD_RES
sequence Y
description Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8

31) chain C
residue 15
type MOD_RES
sequence Y
description Phosphotyrosine; by WEE1 => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507, ECO:0007744|PubMed:19690332
source Swiss-Prot : SWS_FT_FI8

32) chain A
residue 19
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI9

33) chain C
residue 19
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:19369195
source Swiss-Prot : SWS_FT_FI9

34) chain B
residue 211-242
type prosite
sequence RAILVDWLVEVGEEYKLQNETLHLAVNYIDRF
description CYCLINS Cyclins signature. RaiLvdWLvevgeeykLqnetLhlAVnYIDRF
source prosite : PS00292

35) chain A
residue 10-33
type prosite
sequence IGEGTYGVVYKARNKLTGEVVALK
description PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGTYGVVYkArnkltgev..........VALK
source prosite : PS00107

36) chain A
residue 123-135
type prosite
sequence VLHRDLKPQNLLI
description PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI
source prosite : PS00108

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

38) chain C
residue 127
type ACT_SITE
sequence D
description Proton acceptor
source Swiss-Prot : SWS_FT_FI1

39) chain A
residue 132
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI3

40) chain A
residue 145
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI3

41) chain C
residue 132
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI3

42) chain C
residue 145
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI3

43) chain A
residue 160
type MOD_RES
sequence T
description Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995
source Swiss-Prot : SWS_FT_FI10

44) chain C
residue 160
type MOD_RES
sequence T
description Phosphothreonine; by CAK and CCRK => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:14597612, ECO:0000269|PubMed:16325401, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:17570665, ECO:0000269|PubMed:20147522, ECO:0000269|PubMed:20360007, ECO:0000269|PubMed:21565702, ECO:0000305|PubMed:28666995
source Swiss-Prot : SWS_FT_FI10

45) chain A
residue 10
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

46) chain C
residue 129
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

47) chain A
residue 33
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 81
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 86
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 129
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

51) chain C
residue 10
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

52) chain C
residue 33
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

53) chain C
residue 81
type BINDING
sequence E
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

54) chain C
residue 86
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:17095507, ECO:0000269|PubMed:21565702
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI5

56) chain C
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0007744|PubMed:22814378
source Swiss-Prot : SWS_FT_FI5

57) chain A
residue 6
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

58) chain C
residue 6
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0007744|PubMed:19608861
source Swiss-Prot : SWS_FT_FI6

59) chain A
residue 14
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507
source Swiss-Prot : SWS_FT_FI7

60) chain C
residue 14
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:1396589, ECO:0000269|PubMed:17095507
source Swiss-Prot : SWS_FT_FI7


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