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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2BCJ

Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001664molecular_functionG protein-coupled receptor binding
A0002026biological_processregulation of the force of heart contraction
A0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
A0002031biological_processG protein-coupled receptor internalization
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
A0006468biological_processprotein phosphorylation
A0006886biological_processintracellular protein transport
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
A0009966biological_processregulation of signal transduction
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019079biological_processviral genome replication
A0031623biological_processreceptor internalization
A0031694molecular_functionalpha-2A adrenergic receptor binding
A0031755molecular_functionEdg-2 lysophosphatidic acid receptor binding
A0032473cellular_componentcytoplasmic side of mitochondrial outer membrane
A0042995cellular_componentcell projection
A0045202cellular_componentsynapse
A0045880biological_processpositive regulation of smoothened signaling pathway
A0045988biological_processnegative regulation of striated muscle contraction
A0046718biological_processsymbiont entry into host cell
A0047696molecular_functionbeta-adrenergic receptor kinase activity
A0060048biological_processcardiac muscle contraction
A0071880biological_processadenylate cyclase-activating adrenergic receptor signaling pathway
A0098793cellular_componentpresynapse
A0098794cellular_componentpostsynapse
A1901081biological_processnegative regulation of relaxation of smooth muscle
A1903566biological_processpositive regulation of protein localization to cilium
B0001750cellular_componentphotoreceptor outer segment
B0003924molecular_functionGTPase activity
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
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0008283biological_processcell population proliferation
B0016020cellular_componentmembrane
B0030159molecular_functionsignaling receptor complex adaptor activity
B0044877molecular_functionprotein-containing complex binding
B0045202cellular_componentsynapse
B0050909biological_processsensory perception of taste
B0051020molecular_functionGTPase binding
B0060041biological_processretina development in camera-type eye
B0071380biological_processcellular response to prostaglandin E stimulus
B0071870biological_processcellular response to catecholamine stimulus
B0097381cellular_componentphotoreceptor disc membrane
G0003924molecular_functionGTPase activity
G0005515molecular_functionprotein binding
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0007191biological_processadenylate cyclase-activating dopamine receptor signaling pathway
G0016020cellular_componentmembrane
G0031681molecular_functionG-protein beta-subunit binding
G0071380biological_processcellular response to prostaglandin E stimulus
G0071870biological_processcellular response to catecholamine stimulus
Q0000166molecular_functionnucleotide binding
Q0001501biological_processskeletal system development
Q0001508biological_processaction potential
Q0001664molecular_functionG protein-coupled receptor binding
Q0003924molecular_functionGTPase activity
Q0003925molecular_functionG protein activity
Q0005096molecular_functionGTPase activator activity
Q0005515molecular_functionprotein binding
Q0005525molecular_functionGTP binding
Q0005634cellular_componentnucleus
Q0005737cellular_componentcytoplasm
Q0005794cellular_componentGolgi apparatus
Q0005834cellular_componentheterotrimeric G-protein complex
Q0005886cellular_componentplasma membrane
Q0007165biological_processsignal transduction
Q0007186biological_processG protein-coupled receptor signaling pathway
Q0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
Q0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
Q0007207biological_processphospholipase C-activating G protein-coupled acetylcholine receptor signaling pathway
Q0007215biological_processglutamate receptor signaling pathway
Q0007507biological_processheart development
Q0008217biological_processregulation of blood pressure
Q0009791biological_processpost-embryonic development
Q0010543biological_processregulation of platelet activation
Q0016020cellular_componentmembrane
Q0016322biological_processneuron remodeling
Q0016787molecular_functionhydrolase activity
Q0019001molecular_functionguanyl nucleotide binding
Q0021884biological_processforebrain neuron development
Q0030234molecular_functionenzyme regulator activity
Q0030425cellular_componentdendrite
Q0031683molecular_functionG-protein beta/gamma-subunit complex binding
Q0031965cellular_componentnuclear membrane
Q0032024biological_processpositive regulation of insulin secretion
Q0042711biological_processmaternal behavior
Q0042733biological_processembryonic digit morphogenesis
Q0044297cellular_componentcell body
Q0045634biological_processregulation of melanocyte differentiation
Q0046872molecular_functionmetal ion binding
Q0047391molecular_functionalkylglycerophosphoethanolamine phosphodiesterase activity
Q0048066biological_processdevelopmental pigmentation
Q0060158biological_processphospholipase C-activating dopamine receptor signaling pathway
Q0086100biological_processendothelin receptor signaling pathway
Q0099524cellular_componentpostsynaptic cytosol
Q1904888biological_processcranial skeletal system development
Q1990806biological_processligand-gated ion channel signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG Q 361
ChainResidue
QSER53
QTHR186
QGDP360
QALF362
QHOH364
QHOH365
site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE ALF Q 362
ChainResidue
QARG183
QPRO185
QTHR186
QVAL206
QGLY208
QGLN209
QGDP360
QMG361
QHOH363
QHOH364
QHOH365
QGLY48
QGLU49
QLYS52
site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP Q 360
ChainResidue
QGLU49
QSER50
QGLY51
QLYS52
QSER53
QTHR54
QASP155
QSER156
QLEU180
QARG181
QVAL182
QARG183
QASN274
QLYS275
QASP277
QLEU278
QCYS330
QALA331
QTHR332
QMG361
QALF362
QHOH364
QHOH365
QHOH367
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 Residues121
DetailsDomain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues262
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues94
DetailsDomain: {"description":"PH","evidences":[{"source":"PROSITE-ProRule","id":"PRU00145","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues48
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues45
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues40
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues41
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues41
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphohistidine","evidences":[{"source":"PubMed","id":"12486123","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues8
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3FFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20966218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7SQ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1AS0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1GIL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4N0D","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20966218","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7SQ2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsModified residue: {"description":"5-glutamyl histamine","evidences":[{"source":"PubMed","id":"23022564","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
QTHR186
QGLN209
QGLU49
QARG183
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP317
AALA321
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP317
ALYS319
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
QGLN209
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR353
AASP317
ALYS319
site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP317
ALYS319
AASN322
site_idMCSA1
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails

239492

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