Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4MK0

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0001664molecular_functionG protein-coupled receptor binding
A0002026biological_processregulation of the force of heart contraction
A0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
A0003108biological_processnegative regulation of the force of heart contraction by chemical signal
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004703molecular_functionG protein-coupled receptor kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005929cellular_componentcilium
A0006468biological_processprotein phosphorylation
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007213biological_processG protein-coupled acetylcholine receptor signaling pathway
A0007217biological_processtachykinin receptor signaling pathway
A0007507biological_processheart development
A0016020cellular_componentmembrane
A0018105biological_processpeptidyl-serine phosphorylation
A0019079biological_processviral genome replication
A0031623biological_processreceptor internalization
A0031694molecular_functionalpha-2A adrenergic receptor binding
A0031755molecular_functionEdg-2 lysophosphatidic acid receptor binding
A0033605biological_processpositive regulation of catecholamine secretion
A0042995cellular_componentcell projection
A0045202cellular_componentsynapse
A0045988biological_processnegative regulation of striated muscle contraction
A0046718biological_processsymbiont entry into host cell
A0047696molecular_functionbeta-adrenergic receptor kinase activity
A0060048biological_processcardiac muscle contraction
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A1901081biological_processnegative regulation of relaxation of smooth muscle
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005834cellular_componentheterotrimeric G-protein complex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
G0005834cellular_componentheterotrimeric G-protein complex
G0007186biological_processG protein-coupled receptor signaling pathway
G0031681molecular_functionG-protein beta-subunit binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 701
ChainResidue
AGLU653
AHOH806

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE 29X A 702
ChainResidue
ALYS220
ALEU222
AVAL255
AASP272
ALEU273
AMET274
AALA321
ALEU324
ASER334
AASP335
AALA480
AILE197
AARG199
AGLY200
AGLY203
AGLU204
AVAL205
AALA218

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGGFGEVYgCrkadtgkm..........YAMK
ChainResidueDetails
AILE197-LYS220

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvYrDLKpaNILL
ChainResidueDetails
AVAL313-LEU325

site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS
ChainResidueDetails
BLEU70-SER84
BILE157-ILE171
BLEU285-ALA299

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P62873
ChainResidueDetails
BSER2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphohistidine => ECO:0000269|PubMed:12486123
ChainResidueDetails
BHIS266
ALYS220

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon