6KUW
Crystal structure of human alpha2C adrenergic G protein-coupled receptor.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004938 | molecular_function | alpha2-adrenergic receptor activity |
| A | 0006940 | biological_process | regulation of smooth muscle contraction |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0016020 | cellular_component | membrane |
| A | 0019229 | biological_process | regulation of vasoconstriction |
| A | 0030168 | biological_process | platelet activation |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004938 | molecular_function | alpha2-adrenergic receptor activity |
| B | 0006940 | biological_process | regulation of smooth muscle contraction |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0016020 | cellular_component | membrane |
| B | 0019229 | biological_process | regulation of vasoconstriction |
| B | 0030168 | biological_process | platelet activation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue E33 A 1201 |
| Chain | Residue |
| A | TYR127 |
| A | PHE399 |
| A | TYR402 |
| A | PHE419 |
| A | PHE423 |
| A | TYR427 |
| A | ASP131 |
| A | VAL132 |
| A | CYS135 |
| A | LEU204 |
| A | SER214 |
| A | SER218 |
| A | TRP395 |
| A | PHE398 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CLR A 1202 |
| Chain | Residue |
| A | TYR46 |
| A | VAL58 |
| A | PHE64 |
| A | PHE421 |
| A | SER431 |
| A | OLC1207 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 1204 |
| Chain | Residue |
| A | TRP151 |
| A | GLN155 |
| A | GLU158 |
| A | TYR159 |
| A | LYS162 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1205 |
| Chain | Residue |
| A | VAL140 |
| A | CYS143 |
| A | ILE182 |
| A | ILE225 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 1206 |
| Chain | Residue |
| A | LEU88 |
| A | VAL91 |
| A | LYS169 |
| B | TRP209 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue OLC A 1207 |
| Chain | Residue |
| A | GLN45 |
| A | TYR46 |
| A | CLR1202 |
| A | OLA1208 |
| B | GLN413 |
| B | VAL414 |
| B | PRO415 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue OLA A 1208 |
| Chain | Residue |
| A | GLY49 |
| A | ALA50 |
| A | GLY53 |
| A | VAL57 |
| A | ALA170 |
| A | VAL173 |
| A | LEU177 |
| A | OLC1207 |
| B | LEU404 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue OLA A 1209 |
| Chain | Residue |
| A | PHE400 |
| A | SER401 |
| A | GLN413 |
| B | GLN45 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue E33 B 1201 |
| Chain | Residue |
| B | TYR127 |
| B | LEU128 |
| B | ASP131 |
| B | VAL132 |
| B | CYS135 |
| B | LEU204 |
| B | SER214 |
| B | SER218 |
| B | TRP395 |
| B | PHE398 |
| B | PHE399 |
| B | TYR402 |
| B | PHE419 |
| B | PHE423 |
| B | TYR427 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CLR B 1202 |
| Chain | Residue |
| A | LEU418 |
| B | TYR46 |
| B | PHE60 |
| B | PHE421 |
| B | TRP424 |
| B | CYS428 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue OLC B 1203 |
| Chain | Residue |
| B | TYR234 |
| B | PHE382 |
| B | ALA385 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue OLC B 1204 |
| Chain | Residue |
| B | CYS223 |
| B | ALA385 |
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. SSAvHLCAISLDRYWsV |
| Chain | Residue | Details |
| A | SER137-VAL153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 62 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 34 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 50 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 38 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 48 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2019","submissionDatabase":"PDB data bank","title":"Crystal structure of human alpha2C adrenergic G protein-coupled receptor.","authors":["Chen X.Y.","Wu D.","Wu L.J.","Han G.W.","Guo Y.","Zhong G.S."]}},{"source":"PDB","id":"6KUW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Site: {"description":"Implicated in ligand binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Site: {"description":"Implicated in catechol agonist binding and receptor activation","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
