eF-site ID 1h1r-C
PDB Code 1h1r
Chain C

click to enlarge
Title Structure of human Thr160-phospho CDK2/cyclin A complexed with the inhibitor NU6086
Classification TRANSFERASE
Compound CELL DIVISION PROTEIN KINASE 2
Source (CGA2_HUMAN)
Sequence C:  SMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDT
ETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLV
FEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCH
SHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTY
XHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTR
RALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPS
FPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKA
ALAHPFFQDVTKPVPHL
Description (1)  CELL DIVISION PROTEIN KINASE 2 (E.C.2.7.1.-), CYCLIN A2


Functional site

1) chain C
residue 10
type
sequence I
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

2) chain C
residue 12
type
sequence E
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

3) chain C
residue 13
type
sequence G
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

4) chain C
residue 31
type
sequence A
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

5) chain C
residue 80
type
sequence F
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

6) chain C
residue 81
type
sequence E
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

7) chain C
residue 82
type
sequence F
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

8) chain C
residue 83
type
sequence L
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

9) chain C
residue 84
type
sequence H
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

10) chain C
residue 86
type
sequence D
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

11) chain C
residue 89
type
sequence K
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

12) chain C
residue 132
type
sequence N
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

13) chain C
residue 134
type
sequence L
description BINDING SITE FOR RESIDUE 6CP C1298
source : AC2

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

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

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

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

18) 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

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

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

21) chain C
residue 160
type MOD_RES
sequence X
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

22) 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

23) 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

24) 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

25) 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

26) 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

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

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

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

30) 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


Display surface

Download
Links