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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

27EM

Cryo_EM structure of PACAP27_PAC1R_Beta_arrestin 1 complex

Functional Information from PROSITE/UniProt
site_idPS00260
Number of Residues23
DetailsGLUCAGON Glucagon / GIP / secretin / VIP family signature. HSDGIFtDSYsryrkqmaVKKYL
ChainResidueDetails
PHIS1-LEU23
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
ETYR193-HIS199
CTYR204-HIS210
site_idPS00295
Number of Residues19
DetailsARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL
ChainResidueDetails
BPHE61-LEU79
site_idPS00649
Number of Residues25
DetailsG_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CpgmWDnit.CWkpAhvgemvlvsCP
ChainResidueDetails
RCYS54-PRO78
site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFVVaVLYCFlNgeV
ChainResidueDetails
RGLN392-VAL407
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues41
DetailsRegion: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues26
DetailsPeptide: {"description":"Pituitary adenylate cyclase-activating polypeptide 27","featureId":"PRO_0000011489"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsRegion: {"description":"Important for receptor binding","evidences":[{"source":"PubMed","id":"17470806","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Leucine amide","evidences":[{"source":"PubMed","id":"2302217","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues43
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues25
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36385145","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8E3X","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"32004469","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32047270","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6M1I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6P9Y","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues14
DetailsRegion: {"description":"Important for ADCYAP1/PACAP ligand binding and specificity","evidences":[{"source":"PubMed","id":"17470806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21625560","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

259693

PDB entries from 2026-09-16

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