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2XNS

Crystal Structure Of Human G alpha i1 Bound To A Designed Helical Peptide Derived From The Goloco Motif Of RGS14

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
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005794cellular_componentGolgi apparatus
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
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
A0007218biological_processneuropeptide 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
A0034451cellular_componentcentriolar satellite
A0034695biological_processresponse to prostaglandin E
A0036064cellular_componentciliary basal body
A0043434biological_processresponse to peptide hormone
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0070098biological_processchemokine-mediated signaling pathway
A0072678biological_processT cell migration
A1901082biological_processpositive regulation of relaxation of smooth muscle
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001664molecular_functionG protein-coupled receptor binding
B0003924molecular_functionGTPase activity
B0003925molecular_functionG protein activity
B0005515molecular_functionprotein binding
B0005525molecular_functionGTP binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005794cellular_componentGolgi apparatus
B0005813cellular_componentcentrosome
B0005829cellular_componentcytosol
B0005834cellular_componentheterotrimeric G-protein complex
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0007188biological_processadenylate cyclase-modulating G protein-coupled receptor signaling pathway
B0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
B0007193biological_processadenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
B0007198biological_processadenylate cyclase-inhibiting serotonin receptor signaling pathway
B0007218biological_processneuropeptide signaling pathway
B0010854molecular_functionadenylate cyclase regulator activity
B0010855molecular_functionadenylate cyclase inhibitor activity
B0016020cellular_componentmembrane
B0016787molecular_functionhydrolase activity
B0019001molecular_functionguanyl nucleotide binding
B0019003molecular_functionGDP binding
B0030496cellular_componentmidbody
B0031683molecular_functionG-protein beta/gamma-subunit complex binding
B0031749molecular_functionD2 dopamine receptor binding
B0031821molecular_functionG protein-coupled serotonin receptor binding
B0034451cellular_componentcentriolar satellite
B0034695biological_processresponse to prostaglandin E
B0036064cellular_componentciliary basal body
B0043434biological_processresponse to peptide hormone
B0045542biological_processpositive regulation of cholesterol biosynthetic process
B0046676biological_processnegative regulation of insulin secretion
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
B0060236biological_processregulation of mitotic spindle organization
B0070062cellular_componentextracellular exosome
B0070098biological_processchemokine-mediated signaling pathway
B0072678biological_processT cell migration
B1901082biological_processpositive regulation of relaxation of smooth muscle
B1904322biological_processcellular response to forskolin
B1904778biological_processpositive regulation of protein localization to cell cortex
C0030695molecular_functionGTPase regulator activity
D0030695molecular_functionGTPase regulator activity
Functional Information from PDB Data
site_idAC1
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP A 1348
ChainResidue
AGLY42
AARG176
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
CARG516
AGLU43
ASER44
AGLY45
ALYS46
ASER47
ATHR48
AASP150
ASER151

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE GDP B 1348
ChainResidue
BGLY42
BGLU43
BSER44
BGLY45
BLYS46
BSER47
BTHR48
BASP150
BSER151
BARG176
BARG178
BASN269
BLYS270
BASP272
BLEU273
BCYS325
BALA326
BTHR327
DARG516

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 1535
ChainResidue
AGLN147
AARG242
CSER510
CGLY511
CHIS513

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 1535
ChainResidue
BGLN147
BARG242
DSER510
DGLY511
DHIS513

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SRT B 1349
ChainResidue
AGLU275
ATHR295
AGLU297
BLYS271
BHIS322
BPHE323
BASN331
BPHE334
BVAL335

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SRT A 1349
ChainResidue
ALYS271
AHIS322
APHE323
AASN331
APHE334
BGLU275
BTHR295
BTYR296
BGLU297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsRegion: {"description":"G2 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues14
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18434541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22383884","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1KJY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2XNS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21115486","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PDB","id":"1Y3A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2G83","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2GTP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2IK8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2OM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ONW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QE0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3QI2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UMS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4G5Q","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylarginine; by cholera toxin","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Deamidated glutamine; by Photorhabdus PAU_02230","evidences":[{"source":"PubMed","id":"24141704","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues46
DetailsDomain: {"description":"GoLoco","evidences":[{"source":"PROSITE-ProRule","id":"PRU00097","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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