3VW7
Crystal structure of human protease-activated receptor 1 (PAR1) bound with antagonist vorapaxar at 2.2 angstrom
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003796 | molecular_function | lysozyme activity |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0009253 | biological_process | peptidoglycan catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0016998 | biological_process | cell wall macromolecule catabolic process |
| A | 0030430 | cellular_component | host cell cytoplasm |
| A | 0031640 | biological_process | killing of cells of another organism |
| A | 0042742 | biological_process | defense response to bacterium |
| A | 0044659 | biological_process | viral release from host cell by cytolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE VPX A 2001 |
| Chain | Residue |
| A | TYR183 |
| A | LEU332 |
| A | LEU333 |
| A | TYR337 |
| A | ALA349 |
| A | TYR350 |
| A | TYR353 |
| A | HOH3004 |
| A | TYR187 |
| A | PRO236 |
| A | HIS255 |
| A | ASP256 |
| A | VAL257 |
| A | LEU258 |
| A | PHE271 |
| A | ARG1080 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 2002 |
| Chain | Residue |
| A | PHE157 |
| A | TYR206 |
| A | ILE284 |
| A | ARG295 |
| A | OLC2003 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 2003 |
| Chain | Residue |
| A | SER160 |
| A | SER164 |
| A | OLC2002 |
| A | OLC2004 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE OLC A 2004 |
| Chain | Residue |
| A | PHE113 |
| A | PRO156 |
| A | SER160 |
| A | PHE163 |
| A | SER164 |
| A | LEU202 |
| A | LEU229 |
| A | PHE278 |
| A | OLC2003 |
| A | OLC2010 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE OLC A 2005 |
| Chain | Residue |
| A | MET122 |
| A | VAL126 |
| A | PHE127 |
| A | CYS365 |
| A | PRO368 |
| A | TYR371 |
| A | TYR372 |
| A | SER375 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 2006 |
| Chain | Residue |
| A | TRP100 |
| A | PRO328 |
| A | ALA348 |
| A | PHE351 |
| A | CYS356 |
| A | HOH3067 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE OLC A 2007 |
| Chain | Residue |
| A | GLY327 |
| A | PRO328 |
| A | THR343 |
| A | THR346 |
| A | ALA348 |
| A | CYS356 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE OLC A 2008 |
| Chain | Residue |
| A | VAL139 |
| A | HIS143 |
| A | SER220 |
| A | LEU224 |
| A | ALA228 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 2009 |
| Chain | Residue |
| A | PRO236 |
| A | LYS240 |
| A | TYR270 |
| A | PHE271 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 2010 |
| Chain | Residue |
| A | PHE163 |
| A | PHE221 |
| A | THR222 |
| A | OLC2004 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 2011 |
| Chain | Residue |
| A | LYS135 |
| A | LYS307 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 2012 |
| Chain | Residue |
| A | LEU144 |
| A | ASP148 |
| A | SER189 |
| A | ASP367 |
| A | HOH3065 |
| A | HOH3066 |
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. ASIlLMTVISIDRFLaV |
| Chain | Residue | Details |
| A | ALA188-VAL204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04110","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1892846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3382407","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 25 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 61 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 19 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 23 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 2 |
| Details | M-CSA 921 |
| Chain | Residue | Details |
| A | GLU1011 | proton shuttle (general acid/base) |
| A | ASN1020 | covalent catalysis |
