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

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Title Cyclin A binding groove inhibitor Ac-Arg-Arg-Leu-Asn-(m-Cl-Phe)-NH2
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound CELL DIVISION PROTEIN KINASE 2
Source Homo sapiens (Human) (1OKW)
Sequence C:  MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTE
TEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVF
EFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHS
HRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYT
HEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRR
ALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSF
PKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAA
LAHPFFQDVTKPVPHL
Description


Functional site

1) chain C
residue 247
type
sequence D
description BINDING SITE FOR CHAIN F OF ACE-ARG-ARG-LEU-ASN-FCL-NH2
source : AC2

2) 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

3) 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

4) 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

5) 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

6) 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

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

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

9) 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

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

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

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

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

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

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

16) 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

17) 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

18) 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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