2Y4P

Dimeric structure of DAPK-1 catalytic domain

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

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAVVKkCrekstglqyaak......FIKK

Chain	Residue	Details
A	LEU19-LYS46

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

Chain	Residue	Details
A	ILE135-LEU147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP139
B	ASP139
C	ASP139
D	ASP139

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site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING:

Chain	Residue	Details
A	LEU19
B	ASP161
C	LEU19
C	LYS42
C	GLU94
C	GLU100
C	ASP161
D	LEU19
D	LYS42
D	GLU94
D	GLU100
A	LYS42
D	ASP161
A	GLU94
A	GLU100
A	ASP161
B	LEU19
B	LYS42
B	GLU94
B	GLU100

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