9LZ0
Cryo-EM structure of PTH1R-beta-arrestin1 complex in state 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000822 | molecular_function | inositol hexakisphosphate binding |
| A | 0001664 | molecular_function | G protein-coupled receptor binding |
| A | 0001934 | biological_process | positive regulation of protein phosphorylation |
| A | 0002029 | biological_process | desensitization of G protein-coupled receptor signaling pathway |
| A | 0002031 | biological_process | G protein-coupled receptor internalization |
| A | 0002092 | biological_process | positive regulation of receptor internalization |
| A | 0005102 | molecular_function | signaling receptor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005547 | molecular_function | phosphatidylinositol-3,4,5-trisphosphate binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005905 | cellular_component | clathrin-coated pit |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0006898 | biological_process | receptor-mediated endocytosis |
| A | 0007600 | biological_process | sensory perception |
| A | 0008277 | biological_process | regulation of G protein-coupled receptor signaling pathway |
| A | 0009968 | biological_process | negative regulation of signal transduction |
| A | 0030132 | cellular_component | clathrin coat of coated pit |
| A | 0030276 | molecular_function | clathrin binding |
| A | 0031143 | cellular_component | pseudopodium |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0031623 | biological_process | receptor internalization |
| A | 0032050 | molecular_function | clathrin heavy chain binding |
| A | 0033130 | molecular_function | acetylcholine receptor binding |
| A | 0035612 | molecular_function | AP-2 adaptor complex binding |
| A | 0036094 | molecular_function | small molecule binding |
| A | 0045746 | biological_process | negative regulation of Notch signaling pathway |
| A | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0070374 | biological_process | positive regulation of ERK1 and ERK2 cascade |
| A | 0072583 | biological_process | clathrin-dependent endocytosis |
| A | 0097499 | biological_process | protein localization to non-motile cilium |
Functional Information from PROSITE/UniProt
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH |
| Chain | Residue | Details |
| L | TYR193-HIS199 | |
| H | TYR204-HIS210 |
| site_id | PS00295 |
| Number of Residues | 19 |
| Details | ARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL |
| Chain | Residue | Details |
| A | PHE61-LEU79 |
| site_id | PS00649 |
| Number of Residues | 25 |
| Details | G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. ClpeWDhil.CWplGapgevvavpCP |
| Chain | Residue | Details |
| R | CYS108-PRO132 |
| site_id | PS00650 |
| Number of Residues | 16 |
| Details | G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGFFVaIIYCFcNgeV |
| Chain | Residue | Details |
| R | GLN451-VAL466 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 41 |
| Details | Region: {"description":"Interaction with CHRM2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | Topological 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 21 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 21 |
| Details | Topological 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 24 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 19 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 27 |
| Details | Transmembrane: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Motif: {"description":"Important for interaction with G proteins"} |
| Chain | Residue | Details |
