Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3UMS

Crystal structure of the G202A mutant of human G-alpha-i1

Replaces:  2PZ2
Functional Information from GO Data
ChainGOidnamespacecontents
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
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
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
A0034695biological_processresponse to prostaglandin E
A0043434biological_processresponse to peptide hormone
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0070062cellular_componentextracellular exosome
A0072678biological_processT cell migration
A1904322biological_processcellular response to forskolin
A1904778biological_processpositive regulation of protein localization to cell cortex
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE GDP A 355
ChainResidue
AALA41
AARG176
ATHR177
AARG178
AASN269
ALYS270
AASP272
ALEU273
ACYS325
AALA326
ATHR327
AGLU43
AHOH363
AHOH404
AHOH438
AHOH453
AHOH478
ASER44
AGLY45
ALYS46
ASER47
ATHR48
ASER151
ALEU175

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 356
ChainResidue
AARG15
AARG21
AARG32
ALYS180
ALEU348

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486, ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
AGLU43
AASN269

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:18434541, ECO:0000269|PubMed:22383884, ECO:0007744|PDB:3QE0
ChainResidueDetails
ASER47
ATHR181

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ASER151

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1KJY, ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:2XNS, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
ALEU175

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:21115486
ChainResidueDetails
AASP200

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0007744|PDB:1Y3A, ECO:0007744|PDB:2G83, ECO:0007744|PDB:2GTP, ECO:0007744|PDB:2IK8, ECO:0007744|PDB:2OM2, ECO:0007744|PDB:3ONW, ECO:0007744|PDB:3QE0, ECO:0007744|PDB:3QI2, ECO:0007744|PDB:3UMR, ECO:0007744|PDB:3UMS, ECO:0007744|PDB:4G5Q
ChainResidueDetails
AALA326

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250
ChainResidueDetails
AARG178

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704
ChainResidueDetails
AGLN204

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250
ChainResidueDetails
ACYS351

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:20213681, ECO:0000269|PubMed:25255805
ChainResidueDetails
AGLY2

site_idSWS_FT_FI11
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:P10824
ChainResidueDetails
ACYS3

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon