8JJO
Cryo-EM structure of the beta2AR-mBRIL/1b3 Fab/Glue complex with an antagonist
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| F | 0004930 | molecular_function | G protein-coupled receptor activity |
| F | 0004935 | molecular_function | adrenergic receptor activity |
| F | 0004941 | molecular_function | beta2-adrenergic receptor activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0006940 | biological_process | regulation of smooth muscle contraction |
| F | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| F | 0007189 | biological_process | adenylate cyclase-activating G protein-coupled receptor signaling pathway |
| F | 0009055 | molecular_function | electron transfer activity |
| F | 0016020 | cellular_component | membrane |
| F | 0020037 | molecular_function | heme binding |
| F | 0022900 | biological_process | electron transport chain |
| F | 0097746 | biological_process | blood vessel diameter maintenance |
Functional Information from PROSITE/UniProt
| site_id | PS00237 |
| Number of Residues | 17 |
| Details | G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI |
| Chain | Residue | Details |
| F | ALA119-ILE135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 26 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"24056936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4LDE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue"} |
| Chain | Residue | Details |
