5NDZ
Crystal structure of a thermostabilised human protease-activated receptor-2 (PAR2) in complex with AZ3451 at 3.6 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003796 | molecular_function | lysozyme activity |
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 | 0009055 | molecular_function | electron transfer activity |
A | 0009253 | biological_process | peptidoglycan catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0016998 | biological_process | cell wall macromolecule catabolic process |
A | 0020037 | molecular_function | heme binding |
A | 0022900 | biological_process | electron transport chain |
A | 0030430 | cellular_component | host cell cytoplasm |
A | 0031640 | biological_process | killing of cells of another organism |
A | 0042597 | cellular_component | periplasmic space |
A | 0042742 | biological_process | defense response to bacterium |
A | 0044659 | biological_process | viral release from host cell by cytolysis |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue 8UN A 2201 |
Chain | Residue |
A | VAL76 |
A | TYR210 |
A | VAL211 |
A | ALA120 |
A | LEU123 |
A | PHE154 |
A | ALA157 |
A | ASN158 |
A | CYS161 |
A | TRP199 |
A | LEU203 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue NA A 2202 |
Chain | Residue |
A | ASP121 |
A | ASN158 |
A | SER162 |
A | ASN336 |
A | ASP340 |
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 |
site_id | SWS_FT_FI13 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | GLU1011 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | ASP1020 |
site_id | SWS_FT_FI15 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8266098 |
Chain | Residue | Details |
A | LEU1032 | |
A | PHE1104 |
site_id | SWS_FT_FI16 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000303|PubMed:7831309 |
Chain | Residue | Details |
A | SER1117 | |
A | ASN1132 |
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 | ASP1020 | covalent catalysis |