2YA9

Crystal structure of the autoinhibited form of mouse DAPK2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005516	molecular_function	calmodulin binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005794	cellular_component	Golgi apparatus
A	0006468	biological_process	protein phosphorylation
A	0006915	biological_process	apoptotic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0031410	cellular_component	cytoplasmic vesicle
A	0034423	cellular_component	autophagosome lumen
A	0035556	biological_process	intracellular signal transduction
A	0042802	molecular_function	identical protein binding
A	0043065	biological_process	positive regulation of apoptotic process
A	0043276	biological_process	anoikis
A	0090023	biological_process	positive regulation of neutrophil chemotaxis
A	0106310	molecular_function	protein serine kinase activity
A	1990266	biological_process	neutrophil migration
A	2000424	biological_process	positive regulation of eosinophil chemotaxis
A	2001242	biological_process	regulation of intrinsic apoptotic signaling pathway
B	0000166	molecular_function	nucleotide binding
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005516	molecular_function	calmodulin binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005794	cellular_component	Golgi apparatus
B	0006468	biological_process	protein phosphorylation
B	0006915	biological_process	apoptotic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0031410	cellular_component	cytoplasmic vesicle
B	0034423	cellular_component	autophagosome lumen
B	0035556	biological_process	intracellular signal transduction
B	0042802	molecular_function	identical protein binding
B	0043065	biological_process	positive regulation of apoptotic process
B	0043276	biological_process	anoikis
B	0090023	biological_process	positive regulation of neutrophil chemotaxis
B	0106310	molecular_function	protein serine kinase activity
B	1990266	biological_process	neutrophil migration
B	2000424	biological_process	positive regulation of eosinophil chemotaxis
B	2001242	biological_process	regulation of intrinsic apoptotic signaling pathway

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE D1D A 1302

Chain	Residue
A	PHE178
A	GLY179
A	HOH2206
A	HOH2207
B	ILE177
B	D1D1302
B	HOH2206

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1303

Chain	Residue
A	HOH2122
B	ASN190
B	HOH2121
B	HOH2127
A	ASN190
A	HOH2115

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE D1D B 1302

Chain	Residue
A	D1D1302
A	HOH2206
B	PHE178
B	GLY179
B	HOH2206

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU19-LYS46

---

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

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	524
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	18
Details	Region: {"description":"Autoinhibitory domain"}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21497605","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17242355","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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