6KUY
Crystal structure of the alpha2A adrenergic receptor in complex with a partial agonist
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004935 | molecular_function | adrenergic receptor activity |
| A | 0004938 | molecular_function | alpha2-adrenergic receptor activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0006940 | biological_process | regulation of smooth muscle contraction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0016020 | cellular_component | membrane |
| A | 0019229 | biological_process | regulation of vasoconstriction |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0030168 | biological_process | platelet activation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 1201 |
| Chain | Residue |
| A | HIS1063 |
| A | ASP1066 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue E39 A 1202 |
| Chain | Residue |
| A | PHE412 |
| A | TYR416 |
| A | ASP113 |
| A | VAL114 |
| A | CYS117 |
| A | SER204 |
| A | TRP387 |
| A | PHE390 |
| A | PHE391 |
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. SSAwHLCAISLDRYWsI |
| Chain | Residue | Details |
| A | SER119-ILE135 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 35 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 19 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 13 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","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":"35245122","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7EJ0","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Site: {"description":"Implicated in norepinephrine binding","evidences":[{"source":"PubMed","id":"1678850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Site: {"description":"Implicated in catechol and norepinephrine agonist binding and receptor activation","evidences":[{"source":"PubMed","id":"1678850","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Site: {"description":"Implicated in catechol agonist binding and receptor activation","evidences":[{"source":"PubMed","id":"1678850","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Site: {"description":"Implicated in norepinephrine binding and receptor activation","evidences":[{"source":"PubMed","id":"35245122","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P22909","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
