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

7AD3

Class D GPCR Ste2 dimer coupled to two G proteins

Functional Information from GO Data
ChainGOidnamespacecontents
A0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
A0000755biological_processcytogamy
A0004930molecular_functionG protein-coupled receptor activity
A0004932molecular_functionmating-type factor pheromone receptor activity
A0004934molecular_functionmating-type alpha-factor pheromone receptor activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0019236biological_processresponse to pheromone
A0038038cellular_componentG protein-coupled receptor homodimeric complex
B0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
B0000755biological_processcytogamy
B0004930molecular_functionG protein-coupled receptor activity
B0004932molecular_functionmating-type factor pheromone receptor activity
B0004934molecular_functionmating-type alpha-factor pheromone receptor activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007186biological_processG protein-coupled receptor signaling pathway
B0016020cellular_componentmembrane
B0019236biological_processresponse to pheromone
B0038038cellular_componentG protein-coupled receptor homodimeric complex
E0003924molecular_functionGTPase activity
E0005525molecular_functionGTP binding
E0007186biological_processG protein-coupled receptor signaling pathway
E0019001molecular_functionguanyl nucleotide binding
E0031683molecular_functionG-protein beta/gamma-subunit complex binding
F0000749biological_processresponse to pheromone triggering conjugation with cellular fusion
F0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
F0001403biological_processinvasive growth in response to glucose limitation
F0001965molecular_functionG-protein alpha-subunit binding
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005834cellular_componentheterotrimeric G-protein complex
F0005886cellular_componentplasma membrane
F0005937cellular_componentmating projection
F0005938cellular_componentcell cortex
F0007165biological_processsignal transduction
F0007186biological_processG protein-coupled receptor signaling pathway
F0010969biological_processregulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion
F0019236biological_processresponse to pheromone
F0019901molecular_functionprotein kinase binding
F0030159molecular_functionsignaling receptor complex adaptor activity
F0031267molecular_functionsmall GTPase binding
F0031680cellular_componentG-protein beta/gamma-subunit complex
F0031682molecular_functionG-protein gamma-subunit binding
F0043577biological_processchemotropism
F0061951biological_processestablishment of protein localization to plasma membrane
F0097110molecular_functionscaffold protein binding
F0120171cellular_componentCdc24p-Far1p-Gbetagamma complex
F1903260biological_processprotein localization to mating projection tip
G0000750biological_processpheromone-dependent signal transduction involved in conjugation with cellular fusion
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0005834cellular_componentheterotrimeric G-protein complex
G0005886cellular_componentplasma membrane
G0005938cellular_componentcell cortex
G0007165biological_processsignal transduction
G0007186biological_processG protein-coupled receptor signaling pathway
G0010969biological_processregulation of pheromone-dependent signal transduction involved in conjugation with cellular fusion
G0016020cellular_componentmembrane
G0019236biological_processresponse to pheromone
G0031680cellular_componentG-protein beta/gamma-subunit complex
G0031681molecular_functionG-protein beta-subunit binding
G0071944cellular_componentcell periphery
G0120171cellular_componentCdc24p-Far1p-Gbetagamma complex
H0003924molecular_functionGTPase activity
H0005525molecular_functionGTP binding
H0007186biological_processG protein-coupled receptor signaling pathway
H0019001molecular_functionguanyl nucleotide binding
H0031683molecular_functionG-protein beta/gamma-subunit complex binding
I0000772molecular_functionmating pheromone activity
I0005576cellular_componentextracellular region
I0019953biological_processsexual reproduction
K0000772molecular_functionmating pheromone activity
K0005576cellular_componentextracellular region
K0019953biological_processsexual reproduction
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. ILSAsqDgFMLIWDS
ChainResidueDetails
FILE107-SER121
FILE195-ILE209
FMET364-VAL378
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19383463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2K9P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues42
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"1653030","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2017168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19383463","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2K9P","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues106
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"1653030","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"2017168","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11473349","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PJD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"11112532","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11467956","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues16
DetailsMotif: {"description":"Glycine zipper motif","evidences":[{"source":"PubMed","id":"14506226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33268889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues308
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues24
DetailsPeptide: {"description":"Mating factor alpha","featureId":"PRO_0000021700"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues30
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues30
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues29
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues30
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues30
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues13
DetailsRegion: {"description":"G1 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues9
DetailsRegion: {"description":"G3 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues7
DetailsRegion: {"description":"G4 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues5
DetailsRegion: {"description":"G5 motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01230","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P18064","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon