5A6N

Crystal structure of human death associated protein kinase 3 (DAPK3) in complex with compound 2

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE U7E A 300

Chain	Residue
A	GLY20
A	LYS42
A	ILE77
A	ASP161
A	HOH2039
A	HOH2104
A	HOH2183

---

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
B	HIS73
B	PRO74
B	ILE76
B	THR78
B	LYS158
B	HOH2037
A	GLU100
A	ASP103

---

site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PGO A 302

Chain	Residue
A	TYR234
A	ASP235
A	ARG253

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PGO A 303

Chain	Residue
A	ILE209
A	LEU210

---

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 301

Chain	Residue
B	LYS42
B	GLU64
B	ILE77
B	ILE160
B	ASP161
B	PHE162
B	HOH2115

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	28
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGQFAIVRkCrqkgtgkeyaak......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	262
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	43
Details	Region: {"description":"Activation segment","evidences":[{"source":"UniProtKB","id":"O96017","evidenceCode":"ECO:0000250"}]}

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	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J90","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis and ROCK1","evidences":[{"source":"PubMed","id":"15611134","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17158456","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18239682","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---