4MK0

Crystal structure of G protein-coupled receptor kinase 2 in complex with a a rationally designed paroxetine derivative

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001664	molecular_function	G protein-coupled receptor binding
A	0002026	biological_process	regulation of the force of heart contraction
A	0002029	biological_process	desensitization of G protein-coupled receptor signaling pathway
A	0003108	biological_process	negative regulation of the force of heart contraction by chemical signal
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	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005929	cellular_component	cilium
A	0006468	biological_process	protein phosphorylation
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007213	biological_process	G protein-coupled acetylcholine receptor signaling pathway
A	0007217	biological_process	tachykinin receptor signaling pathway
A	0007507	biological_process	heart development
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019079	biological_process	viral genome replication
A	0031623	biological_process	receptor internalization
A	0031694	molecular_function	alpha-2A adrenergic receptor binding
A	0031755	molecular_function	Edg-2 lysophosphatidic acid receptor binding
A	0032473	cellular_component	cytoplasmic side of mitochondrial outer membrane
A	0033605	biological_process	positive regulation of catecholamine secretion
A	0042995	cellular_component	cell projection
A	0045202	cellular_component	synapse
A	0045988	biological_process	negative regulation of striated muscle contraction
A	0046718	biological_process	symbiont entry into host cell
A	0047696	molecular_function	beta-adrenergic receptor kinase activity
A	0060048	biological_process	cardiac muscle contraction
A	0098793	cellular_component	presynapse
A	0098794	cellular_component	postsynapse
A	1901081	biological_process	negative regulation of relaxation of smooth muscle
B	0001750	cellular_component	photoreceptor outer segment
B	0003924	molecular_function	GTPase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005834	cellular_component	heterotrimeric G-protein complex
B	0007165	biological_process	signal transduction
B	0007186	biological_process	G protein-coupled receptor signaling pathway
B	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
B	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
B	0008283	biological_process	cell population proliferation
B	0016020	cellular_component	membrane
B	0030159	molecular_function	signaling receptor complex adaptor activity
B	0044877	molecular_function	protein-containing complex binding
B	0045202	cellular_component	synapse
B	0050909	biological_process	sensory perception of taste
B	0051020	molecular_function	GTPase binding
B	0060041	biological_process	retina development in camera-type eye
B	0071380	biological_process	cellular response to prostaglandin E stimulus
B	0071870	biological_process	cellular response to catecholamine stimulus
B	0097381	cellular_component	photoreceptor disc membrane
G	0005834	cellular_component	heterotrimeric G-protein complex
G	0007186	biological_process	G protein-coupled receptor signaling pathway
G	0031681	molecular_function	G-protein beta-subunit binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 701

Chain	Residue
A	GLU653
A	HOH806

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 29X A 702

Chain	Residue
A	LYS220
A	LEU222
A	VAL255
A	ASP272
A	LEU273
A	MET274
A	ALA321
A	LEU324
A	SER334
A	ASP335
A	ALA480
A	ILE197
A	ARG199
A	GLY200
A	GLY203
A	GLU204
A	VAL205
A	ALA218

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE197-LYS220

---

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

Chain	Residue	Details
A	VAL313-LEU325

---

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS

Chain	Residue	Details
B	LEU70-SER84
B	ILE157-ILE171
B	LEU285-ALA299

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	121
Details	Domain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	94
Details	Domain: {"description":"PH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
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	9
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	48
Details	Repeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	45
Details	Repeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	40
Details	Repeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	41
Details	Repeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	43
Details	Repeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	41
Details	Repeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	30
Details	Repeat: {"description":"WD 7","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	Modified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"12486123","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---