eF-site ID 4fx3-C
PDB Code 4fx3
Chain C

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Title Crystal Structure of the CDK2/Cyclin A complex with oxindole inhibitor
Classification transferase/transferase inhibitor
Compound Cyclin-dependent kinase 2
Source Homo sapiens (Human) (CCNA2_HUMAN)
Sequence C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHLRL
Description


Functional site

1) chain C
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

2) chain C
residue 31
type
sequence A
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

3) chain C
residue 33
type
sequence K
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

4) chain C
residue 80
type
sequence F
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

5) chain C
residue 81
type
sequence E
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

6) chain C
residue 82
type
sequence F
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

7) chain C
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

8) chain C
residue 84
type
sequence H
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

9) chain C
residue 85
type
sequence Q
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

10) chain C
residue 86
type
sequence D
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

11) chain C
residue 89
type
sequence K
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

12) chain C
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

13) chain C
residue 145
type
sequence D
description BINDING SITE FOR RESIDUE 60K C 301
source : AC4

14) 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

15) 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

16) 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

17) 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

18) 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

19) 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

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

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

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

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

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

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

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

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

28) 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

29) 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

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


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