5NJ6
Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in ternary complex with Fab3949 and AZ7188 at 4.0 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004930 | molecular_function | G protein-coupled receptor activity |
A | 0005506 | molecular_function | iron ion binding |
A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
A | 0007596 | biological_process | blood coagulation |
A | 0009055 | molecular_function | electron transfer activity |
A | 0015057 | molecular_function | thrombin-activated receptor activity |
A | 0016020 | cellular_component | membrane |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0042597 | cellular_component | periplasmic space |
A | 0046872 | molecular_function | metal ion binding |
A | 0070493 | biological_process | thrombin-activated receptor signaling pathway |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
Chain | Residue | Details |
L | TYR192-HIS198 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 29 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | LYS72-LEU101 |
site_id | SWS_FT_FI2 |
Number of Residues | 11 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | PHE102-ALA108 | |
A | VAL178-HIS183 |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | PRO109-HIS137 |
site_id | SWS_FT_FI4 |
Number of Residues | 39 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | GLY138-ASN149 | |
A | VAL212-LEU235 | |
A | GLY318-TYR323 |
site_id | SWS_FT_FI5 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | VAL150-ILE177 |
site_id | SWS_FT_FI6 |
Number of Residues | 27 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | SER184-VAL211 |
site_id | SWS_FT_FI7 |
Number of Residues | 33 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | VAL236-LEU269 |
site_id | SWS_FT_FI8 |
Number of Residues | 39 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | SER278-GLN317 |
site_id | SWS_FT_FI9 |
Number of Residues | 23 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:28445455 |
Chain | Residue | Details |
A | ALA324-VAL347 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21627585 |
Chain | Residue | Details |
A | CYS361 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12171601 |
Chain | Residue | Details |
A | GLN222 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | TRP2006 | |
A | ILE2101 |