5VJA

Crystal Structure of human zipper-interacting protein kinase (ZIPK, alias DAPK3) in complex with a pyrazolo[3,4-d]pyrimidinone ligand (HS38)

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 PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue DMS A 1001

Chain	Residue
A	ILE177
A	PHE178
A	PRO181
A	LEU226
A	HOH1122

---

site_id	AC2
Number of Residues	13
Details	binding site for residue DUK A 1002

Chain	Residue
A	LEU93
A	VAL96
A	MET146
A	ILE160
A	ASP161
A	HOH1109
A	HOH1158
A	HOH1161
A	HOH1175
A	LEU19
A	GLY20
A	VAL27
A	LYS42

---

site_id	AC3
Number of Residues	4
Details	binding site for residue DMS B 1001

Chain	Residue
B	ILE177
B	PHE178
B	GLY179
B	PRO181

---

site_id	AC4
Number of Residues	10
Details	binding site for residue DUK B 1002

Chain	Residue
B	LEU19
B	VAL27
B	LYS42
B	LEU93
B	VAL96
B	ASP161
B	HOH1110
B	HOH1132
B	HOH1148
B	HOH1233

---

site_id	AC5
Number of Residues	3
Details	binding site for residue DMS C 1001

Chain	Residue
C	ILE177
C	GLY179
C	HOH1191

---

site_id	AC6
Number of Residues	11
Details	binding site for residue DUK C 1002

Chain	Residue
C	LEU19
C	GLY22
C	LYS42
C	LEU93
C	MET146
C	ILE160
C	ASP161
C	HOH1117
C	HOH1136
C	HOH1163
C	HOH1192

---

site_id	AC7
Number of Residues	3
Details	binding site for residue ILE D 301

Chain	Residue
D	ILE275
D	LYS276
D	ALA277

---

site_id	AC8
Number of Residues	3
Details	binding site for residue DMS D 302

Chain	Residue
D	PHE178
D	GLY179
D	HOH492

---

site_id	AC9
Number of Residues	9
Details	binding site for residue DUK D 303

Chain	Residue
D	LEU19
D	GLY22
D	VAL27
D	LYS42
D	LEU93
D	MET146
D	ILE160
D	ASP161
D	HOH429

---

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	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

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU19
B	LEU19
C	LEU19
D	LEU19

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305

Chain	Residue	Details
A	LYS42
B	LYS42
C	LYS42
D	LYS42

---

site_id	SWS_FT_FI4
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:18239682, ECO:0007744|PDB:2J90

Chain	Residue	Details
A	GLU94
A	VAL96
B	GLU94
B	VAL96
C	GLU94
C	VAL96
D	GLU94
D	VAL96

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	SER50
B	SER50
C	SER50
D	SER50

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456

Chain	Residue	Details
A	THR180
B	THR180
C	THR180
D	THR180

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269|PubMed:15611134

Chain	Residue	Details
A	THR225
B	THR225
C	THR225
D	THR225

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphothreonine; by autocatalysis and ROCK1 => ECO:0000269|PubMed:15611134, ECO:0000269|PubMed:17158456, ECO:0000269|PubMed:18239682

Chain	Residue	Details
A	THR265
B	THR265
C	THR265
D	THR265

---