4L9I

Bovine G Protein Coupled Receptor Kinase 1 in Complex with Paroxetine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001750	cellular_component	photoreceptor outer segment
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004703	molecular_function	G protein-coupled receptor kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
A	0007601	biological_process	visual perception
A	0009966	biological_process	regulation of signal transduction
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0022400	biological_process	regulation of opsin-mediated signaling pathway
A	0050254	molecular_function	rhodopsin kinase activity
A	0097381	cellular_component	photoreceptor disc membrane
B	0000166	molecular_function	nucleotide binding
B	0001750	cellular_component	photoreceptor outer segment
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004703	molecular_function	G protein-coupled receptor kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0006468	biological_process	protein phosphorylation
B	0007165	biological_process	signal transduction
B	0007601	biological_process	visual perception
B	0009966	biological_process	regulation of signal transduction
B	0016020	cellular_component	membrane
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0022400	biological_process	regulation of opsin-mediated signaling pathway
B	0050254	molecular_function	rhodopsin kinase activity
B	0097381	cellular_component	photoreceptor disc membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE 8PR A 601

Chain	Residue
A	GLY194
A	ASP271
A	GLU318
A	LEU321
A	ARG195
A	GLY196
A	GLY199
A	VAL201
A	ALA214
A	LEU218
A	THR265
A	MET267

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MES A 602

Chain	Residue
A	ASP127
A	ALA128
A	GLU129
A	GLY348
A	TYR349
A	ALA350

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE 8PR B 601

Chain	Residue
B	GLY194
B	ARG195
B	GLY196
B	GLY199
B	VAL201
B	ALA214
B	THR265
B	MET267
B	ASP271
B	GLU318
B	LEU321

---

site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL B 602

Chain	Residue
A	GLN173
B	LEU166

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL B 603

Chain	Residue
A	SER165
A	LEU166
B	ARG170
B	GLN173

---

Functional Information from PROSITE/UniProt

site_id	PS00107
Number of Residues	24
Details	PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGGFGEVFaCqmkatgkl..........YACK

Chain	Residue	Details
A	LEU193-LYS216

---

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

Chain	Residue	Details
A	ILE310-LEU322

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	228
Details	Domain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	530
Details	Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	65
Details	Domain: {"description":"AGC-kinase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00618","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"1527025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"1527025","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18339619","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---