eF-site ID 6q4e-A
PDB Code 6q4e
Chain A

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Title CDK2 in complex with FragLite33
Classification CELL CYCLE
Compound Cyclin-dependent kinase 2
Source (CDK2_HUMAN)
Sequence A:  FMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLPS
TAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQD
LKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHR
DLKPQNLLINTEGAIKLADFGLARAFGEVVTLWYRAPEIL
LGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFR
IFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPP
LDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVP
HLRL
Description


Functional site

1) chain A
residue 3
type
sequence N
description binding site for residue DMS A 301
source : AC1

2) chain A
residue 4
type
sequence F
description binding site for residue DMS A 301
source : AC1

3) chain A
residue 72
type
sequence T
description binding site for residue DMS A 301
source : AC1

4) chain A
residue 77
type
sequence Y
description binding site for residue DMS A 301
source : AC1

5) chain A
residue 219
type
sequence L
description binding site for residue DMS A 302
source : AC2

6) chain A
residue 220
type
sequence G
description binding site for residue DMS A 302
source : AC2

7) chain A
residue 221
type
sequence T
description binding site for residue DMS A 302
source : AC2

8) chain A
residue 223
type
sequence D
description binding site for residue DMS A 302
source : AC2

9) chain A
residue 245
type
sequence R
description binding site for residue DMS A 302
source : AC2

10) chain A
residue 269
type
sequence Y
description binding site for residue DMS A 302
source : AC2

11) chain A
residue 10
type
sequence I
description binding site for residue HH5 A 303
source : AC3

12) chain A
residue 31
type
sequence A
description binding site for residue HH5 A 303
source : AC3

13) chain A
residue 33
type
sequence K
description binding site for residue HH5 A 303
source : AC3

14) chain A
residue 64
type
sequence V
description binding site for residue HH5 A 303
source : AC3

15) chain A
residue 80
type
sequence F
description binding site for residue HH5 A 303
source : AC3

16) chain A
residue 81
type
sequence E
description binding site for residue HH5 A 303
source : AC3

17) chain A
residue 82
type
sequence F
description binding site for residue HH5 A 303
source : AC3

18) chain A
residue 83
type
sequence L
description binding site for residue HH5 A 303
source : AC3

19) chain A
residue 134
type
sequence L
description binding site for residue HH5 A 303
source : AC3

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

21) 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

22) 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

23) 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

24) 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

25) 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

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

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

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

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

30) 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

31) 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

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

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

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

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

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

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


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