Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1AGR

COMPLEX OF ALF4-ACTIVATED GI-ALPHA-1 WITH RGS4

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001664molecular_functionG protein-coupled receptor binding
A0003924molecular_functionGTPase activity
A0003925molecular_functionG protein activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005829cellular_componentcytosol
A0005834cellular_componentheterotrimeric G-protein complex
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
A0010854molecular_functionadenylate cyclase regulator activity
A0010855molecular_functionadenylate cyclase inhibitor activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0019001molecular_functionguanyl nucleotide binding
A0019003molecular_functionGDP binding
A0030496cellular_componentmidbody
A0031683molecular_functionG-protein beta/gamma-subunit complex binding
A0031749molecular_functionD2 dopamine receptor binding
A0031821molecular_functionG protein-coupled serotonin receptor binding
A0032794molecular_functionGTPase activating protein binding
A0032991cellular_componentprotein-containing complex
A0034695biological_processresponse to prostaglandin E
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0050805biological_processnegative regulation of synaptic transmission
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0072678biological_processT cell migration
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0001664molecular_functionG protein-coupled receptor binding
D0003924molecular_functionGTPase activity
D0003925molecular_functionG protein activity
D0005515molecular_functionprotein binding
D0005525molecular_functionGTP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005829cellular_componentcytosol
D0005834cellular_componentheterotrimeric G-protein complex
D0005856cellular_componentcytoskeleton
D0005886cellular_componentplasma membrane
D0005938cellular_componentcell cortex
D0007165biological_processsignal transduction
D0007186biological_processG protein-coupled receptor signaling pathway
D0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
D0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
D0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
D0010854molecular_functionadenylate cyclase regulator activity
D0010855molecular_functionadenylate cyclase inhibitor activity
D0016020cellular_componentmembrane
D0016787molecular_functionhydrolase activity
D0019001molecular_functionguanyl nucleotide binding
D0019003molecular_functionGDP binding
D0030496cellular_componentmidbody
D0031683molecular_functionG-protein beta/gamma-subunit complex binding
D0031749molecular_functionD2 dopamine receptor binding
D0031821molecular_functionG protein-coupled serotonin receptor binding
D0032794molecular_functionGTPase activating protein binding
D0032991cellular_componentprotein-containing complex
D0034695biological_processresponse to prostaglandin E
D0045542biological_processpositive regulation of cholesterol biosynthetic process
D0046676biological_processnegative regulation of insulin secretion
D0046872molecular_functionmetal ion binding
D0050805biological_processnegative regulation of synaptic transmission
D0051301biological_processcell division
D0060236biological_processregulation of mitotic spindle organization
D0072678biological_processT cell migration
D0098794cellular_componentpostsynapse
D0098978cellular_componentglutamatergic synapse
D0099645biological_processneurotransmitter receptor localization to postsynaptic specialization membrane
D1904322biological_processcellular response to forskolin
D1904778biological_processpositive regulation of protein localization to cell cortex
E0001965molecular_functionG-protein alpha-subunit binding
E0001975biological_processresponse to amphetamine
E0005096molecular_functionGTPase activator activity
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0009968biological_processnegative regulation of signal transduction
E0010460biological_processpositive regulation of heart rate
E0019901molecular_functionprotein kinase binding
E0032991cellular_componentprotein-containing complex
E0042220biological_processresponse to cocaine
E0045471biological_processresponse to ethanol
E0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
E0051924biological_processregulation of calcium ion transport
E0060160biological_processnegative regulation of dopamine receptor signaling pathway
E0061052biological_processnegative regulation of cell growth involved in cardiac muscle cell development
E0110053biological_processregulation of actin filament organization
E1900924biological_processnegative regulation of glycine import across plasma membrane
E1901379biological_processregulation of potassium ion transmembrane transport
E1901380biological_processnegative regulation of potassium ion transmembrane transport
E1990791biological_processdorsal root ganglion development
E2000463biological_processpositive regulation of excitatory postsynaptic potential
H0001965molecular_functionG-protein alpha-subunit binding
H0001975biological_processresponse to amphetamine
H0005096molecular_functionGTPase activator activity
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0009968biological_processnegative regulation of signal transduction
H0010460biological_processpositive regulation of heart rate
H0019901molecular_functionprotein kinase binding
H0032991cellular_componentprotein-containing complex
H0042220biological_processresponse to cocaine
H0045471biological_processresponse to ethanol
H0045744biological_processnegative regulation of G protein-coupled receptor signaling pathway
H0051924biological_processregulation of calcium ion transport
H0060160biological_processnegative regulation of dopamine receptor signaling pathway
H0061052biological_processnegative regulation of cell growth involved in cardiac muscle cell development
H0110053biological_processregulation of actin filament organization
H1900924biological_processnegative regulation of glycine import across plasma membrane
H1901379biological_processregulation of potassium ion transmembrane transport
H1901380biological_processnegative regulation of potassium ion transmembrane transport
H1990791biological_processdorsal root ganglion development
H2000463biological_processpositive regulation of excitatory postsynaptic potential
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 356
ChainResidue
ASER47
ATHR181
AGDP355
AALF357
AHOH364
AHOH365
site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ALF A 357
ChainResidue
AARG178
ALYS180
ATHR181
AVAL201
AGLY202
AGLY203
AGLN204
AGDP355
AMG356
AHOH359
AHOH364
AHOH365
AGLY42
AGLU43
ALYS46
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG D 356
ChainResidue
DSER47
DTHR181
DGDP355
DALF357
DHOH365
DHOH366
site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ALF D 357
ChainResidue
DGLY42
DGLU43
DLYS46
DARG178
DLYS180
DTHR181
DVAL201
DGLY202
DGLY203
DGLN204
DGDP355
DMG356
DHOH360
DHOH365
DHOH366
site_idAC5
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AMG356
AALF357
AHOH360
AHOH361
AHOH364
AHOH365
site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE CIT A 358
ChainResidue
AGLU275
ATHR295
ATYR296
AGLU297
AHOH384
DLYS271
DHIS322
DPHE323
DASN331
DPHE334
DHOH384
site_idAC7
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP D 355
ChainResidue
DHOH365
DHOH366
DGLU43
DSER44
DGLY45
DLYS46
DSER47
DTHR48
DSER151
DLEU175
DARG176
DTHR177
DARG178
DASN269
DLYS270
DASP272
DLEU273
DCYS325
DALA326
DTHR327
DMG356
DALF357
DHOH361
DHOH362
site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE CIT D 358
ChainResidue
ALYS271
AHIS322
APHE323
AASN331
DGLU275
DTHR295
DTYR296
DGLU297
DHOH359
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues644
DetailsDomain: {"description":"G-alpha","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues26
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues16
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues18
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues14
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues10
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues30
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_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
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_FI10
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19703466","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25037222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9705312","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BH2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PAO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1AS0","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_FI12
Number of Residues116
DetailsDomain: {"description":"RGS","evidences":[{"source":"PROSITE-ProRule","id":"PRU00171","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR181
AGLN204
AGLU43
AARG178
site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DTHR181
DGLN204
DGLU43
DARG178
site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
AGLN204
site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
DGLN204
site_idMCSA1
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails
AGLU43electrostatic stabiliser
ATHR48electrostatic stabiliser
AARG178electrostatic stabiliser
AASP200electrostatic stabiliser
AGLN204electrostatic stabiliser
site_idMCSA2
Number of Residues5
DetailsM-CSA 533
ChainResidueDetails

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon