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

9LY3

A Cryo-EM structure of LA-PTH-PTH1R-V2RT-Beta-arrestin1 complex (state 2 conformation)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005179molecular_functionhormone activity
A0005576cellular_componentextracellular region
A0030282biological_processbone mineralization
B0000139cellular_componentGolgi membrane
B0000785cellular_componentchromatin
B0001664molecular_functionG protein-coupled receptor binding
B0001678biological_processintracellular glucose homeostasis
B0001934biological_processpositive regulation of protein phosphorylation
B0002029biological_processdesensitization of G protein-coupled receptor signaling pathway
B0002031biological_processG protein-coupled receptor internalization
B0002092biological_processpositive regulation of receptor internalization
B0003713molecular_functiontranscription coactivator activity
B0004402molecular_functionhistone acetyltransferase activity
B0004857molecular_functionenzyme inhibitor activity
B0004869molecular_functioncysteine-type endopeptidase inhibitor activity
B0005096molecular_functionGTPase activator activity
B0005159molecular_functioninsulin-like growth factor receptor binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005765cellular_componentlysosomal membrane
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005905cellular_componentclathrin-coated pit
B0005929cellular_componentcilium
B0006357biological_processregulation of transcription by RNA polymerase II
B0006511biological_processubiquitin-dependent protein catabolic process
B0007165biological_processsignal transduction
B0007166biological_processcell surface receptor signaling pathway
B0007600biological_processsensory perception
B0016567biological_processprotein ubiquitination
B0019899molecular_functionenzyme binding
B0030659cellular_componentcytoplasmic vesicle membrane
B0030666cellular_componentendocytic vesicle membrane
B0030674molecular_functionprotein-macromolecule adaptor activity
B0031143cellular_componentpseudopodium
B0031410cellular_componentcytoplasmic vesicle
B0031434molecular_functionmitogen-activated protein kinase kinase binding
B0031625molecular_functionubiquitin protein ligase binding
B0031701molecular_functionangiotensin receptor binding
B0032715biological_processnegative regulation of interleukin-6 production
B0032717biological_processnegative regulation of interleukin-8 production
B0035025biological_processpositive regulation of Rho protein signal transduction
B0035721biological_processintraciliary retrograde transport
B0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
B0042981biological_processregulation of apoptotic process
B0043124biological_processnegative regulation of canonical NF-kappaB signal transduction
B0043149biological_processstress fiber assembly
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0045746biological_processnegative regulation of Notch signaling pathway
B0045880biological_processpositive regulation of smoothened signaling pathway
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0060090molecular_functionmolecular adaptor activity
B0070374biological_processpositive regulation of ERK1 and ERK2 cascade
B0097499biological_processprotein localization to non-motile cilium
B1902533biological_processpositive regulation of intracellular signal transduction
B1903568biological_processnegative regulation of protein localization to ciliary membrane
B1990763molecular_functionarrestin family protein binding
R0004888molecular_functiontransmembrane signaling receptor activity
R0004930molecular_functionG protein-coupled receptor activity
R0004991molecular_functionparathyroid hormone receptor activity
R0007166biological_processcell surface receptor signaling pathway
R0007186biological_processG protein-coupled receptor signaling pathway
R0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
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. ClpeWDhil.CWplGapgevvavpCP
ChainResidueDetails
RCYS108-PRO132

site_idPS00650
Number of Residues16
DetailsG_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVaIIYCFcNgeV
ChainResidueDetails
RGLN451-VAL466

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 Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"37209686","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8GOC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8I10","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues7
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"30975883","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NBF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NBI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

257629

PDB entries from 2026-08-05

PDB statisticsPDBj update infoContact PDBjnumon