3I6W

Structure and Activation Mechanism of the CHK2 DNA-Damage Checkpoint Kinase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004672	molecular_function	protein kinase activity
A	0005524	molecular_function	ATP binding
A	0006468	biological_process	protein phosphorylation
B	0004672	molecular_function	protein kinase activity
B	0005524	molecular_function	ATP binding
B	0006468	biological_process	protein phosphorylation
C	0004672	molecular_function	protein kinase activity
C	0005524	molecular_function	ATP binding
C	0006468	biological_process	protein phosphorylation
D	0004672	molecular_function	protein kinase activity
D	0005524	molecular_function	ATP binding
D	0006468	biological_process	protein phosphorylation
E	0004672	molecular_function	protein kinase activity
E	0005524	molecular_function	ATP binding
E	0006468	biological_process	protein phosphorylation
F	0004672	molecular_function	protein kinase activity
F	0005524	molecular_function	ATP binding
F	0006468	biological_process	protein phosphorylation
G	0004672	molecular_function	protein kinase activity
G	0005524	molecular_function	ATP binding
G	0006468	biological_process	protein phosphorylation
H	0004672	molecular_function	protein kinase activity
H	0005524	molecular_function	ATP binding
H	0006468	biological_process	protein phosphorylation

Functional Information from PROSITE/UniProt

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNVLL

Chain	Residue	Details
A	ILE343-LEU355

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP347
B	ASP347
C	ASP347
D	ASP347
E	ASP347
F	ASP347
G	ASP347
H	ASP347

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site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING:

Chain	Residue	Details
A	GLY227
B	ASP368
C	GLY227
C	ARG249
C	GLU302
C	GLU351
C	ASP368
D	GLY227
D	ARG249
D	GLU302
D	GLU351
A	ARG249
D	ASP368
E	GLY227
E	ARG249
E	GLU302
E	GLU351
E	ASP368
F	GLY227
F	ARG249
F	GLU302
F	GLU351
A	GLU302
F	ASP368
G	GLY227
G	ARG249
G	GLU302
G	GLU351
G	ASP368
H	GLY227
H	ARG249
H	GLU302
H	GLU351
A	GLU351
H	ASP368
A	ASP368
B	GLY227
B	ARG249
B	GLU302
B	GLU351

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site_id	SWS_FT_FI3
Number of Residues	8
Details	MOD_RES: Phosphoserine; by PLK3 => ECO:0000269|PubMed:16481012

Chain	Residue	Details
A	SER73
B	SER73
C	SER73
D	SER73
E	SER73
F	SER73
G	SER73
H	SER73

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site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18644861

Chain	Residue	Details
A	SER379
B	SER379
C	SER379
D	SER379
E	SER379
F	SER379
G	SER379
H	SER379

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site_id	SWS_FT_FI5
Number of Residues	16
Details	MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:11390408

Chain	Residue	Details
A	THR383
E	THR387
F	THR383
F	THR387
G	THR383
G	THR387
H	THR383
H	THR387
A	THR387
B	THR383
B	THR387
C	THR383
C	THR387
D	THR383
D	THR387
E	THR383

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:17715138

Chain	Residue	Details
A	SER456
B	SER456
C	SER456
D	SER456
E	SER456
F	SER456
G	SER456
H	SER456

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