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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9WSV

Cryo-EM structure of DAMGO-muOR-arrestin-1-Fab30 complex

Functional Information from GO Data
ChainGOidnamespacecontents
C0000822molecular_functioninositol hexakisphosphate binding
C0001664molecular_functionG protein-coupled receptor binding
C0001934biological_processpositive regulation of protein phosphorylation
C0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
C0002031biological_processG protein-coupled receptor internalization
C0002092biological_processpositive regulation of receptor internalization
C0005515molecular_functionprotein binding
C0005547molecular_functionphosphatidylinositol-3,4,5-trisphosphate binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0005905cellular_componentclathrin-coated pit
C0006351biological_processDNA-templated transcription
C0006511biological_processubiquitin-dependent protein catabolic process
C0006898biological_processreceptor-mediated endocytosis
C0007600biological_processsensory perception
C0008277biological_processregulation of G protein-coupled receptor signaling pathway
C0009968biological_processnegative regulation of signal transduction
C0015031biological_processprotein transport
C0030132cellular_componentclathrin coat of coated pit
C0030276molecular_functionclathrin binding
C0031143cellular_componentpseudopodium
C0031410cellular_componentcytoplasmic vesicle
C0031623biological_processreceptor internalization
C0032050molecular_functionclathrin heavy chain binding
C0033130molecular_functionacetylcholine receptor binding
C0035612molecular_functionAP-2 adaptor complex binding
C0036094molecular_functionsmall molecule binding
C0045746biological_processnegative regulation of Notch signaling pathway
C0060090molecular_functionmolecular adaptor activity
C0070374biological_processpositive regulation of ERK1 and ERK2 cascade
C0072583biological_processclathrin-dependent endocytosis
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. TSIfTLCTMSVDRYIaV
ChainResidueDetails
RTHR153-VAL169
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
HTYR204-HIS210
LTYR193-HIS199
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
CPHE61-LEU79
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues36
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues14
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues31
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues39
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"22437502","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsMotif: {"description":"NPxxY; plays a role in stabilizing the activated conformation of the receptor","evidences":[{"source":"PubMed","id":"26245379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P33535","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues41
DetailsRegion: {"description":"Interaction with CHRM2"}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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