4XNW
The human P2Y1 receptor in complex with MRS2500
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 | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
A | 0009055 | molecular_function | electron transfer activity |
A | 0016020 | cellular_component | membrane |
A | 0030168 | biological_process | platelet activation |
A | 0043448 | biological_process | alkane catabolic process |
A | 0045028 | molecular_function | G protein-coupled purinergic nucleotide receptor activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0090075 | biological_process | relaxation of muscle |
C | 0004930 | molecular_function | G protein-coupled receptor activity |
C | 0005506 | molecular_function | iron ion binding |
C | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
C | 0007200 | biological_process | phospholipase C-activating G protein-coupled receptor signaling pathway |
C | 0009055 | molecular_function | electron transfer activity |
C | 0016020 | cellular_component | membrane |
C | 0030168 | biological_process | platelet activation |
C | 0043448 | biological_process | alkane catabolic process |
C | 0045028 | molecular_function | G protein-coupled purinergic nucleotide receptor activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0090075 | biological_process | relaxation of muscle |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | binding site for residue 2ID A 1101 |
Chain | Residue |
A | CYS42 |
A | ASN283 |
A | ALA286 |
A | ARG287 |
A | GLN291 |
A | ASN299 |
A | TYR303 |
A | TYR306 |
A | ARG310 |
A | HOH1202 |
A | HOH1205 |
A | LEU44 |
A | LYS46 |
A | TYR110 |
A | ARG195 |
A | THR201 |
A | TYR203 |
A | ASP204 |
A | THR205 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN A 1102 |
Chain | Residue |
A | CYS1006 |
A | CYS1009 |
A | CYS1039 |
A | CYS1042 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue 2ID C 1101 |
Chain | Residue |
C | LYS46 |
C | TYR110 |
C | ARG195 |
C | THR201 |
C | ASP204 |
C | THR205 |
C | ASN283 |
C | ALA286 |
C | ARG287 |
C | GLN291 |
C | ASN299 |
C | TYR303 |
C | TYR306 |
C | ARG310 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN C 1102 |
Chain | Residue |
C | CYS1006 |
C | CYS1009 |
C | CYS1039 |
C | CYS1042 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | TYR52-TRP74 | |
C | TYR52-TRP74 |
site_id | SWS_FT_FI2 |
Number of Residues | 154 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | MET75-SER87 | |
A | HIS148-LYS166 | |
A | LEU326-LEU373 | |
C | MET75-SER87 | |
C | HIS148-LYS166 | |
C | LEU326-LEU373 |
site_id | SWS_FT_FI3 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | VAL88-PHE109 | |
C | VAL88-PHE109 |
site_id | SWS_FT_FI4 |
Number of Residues | 116 |
Details | TOPO_DOM: Extracellular => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | TYR110-LYS125 | |
A | TYR189-TYR214 | |
A | ARG285-TYR303 | |
C | TYR110-LYS125 | |
C | TYR189-TYR214 | |
C | ARG285-TYR303 |
site_id | SWS_FT_FI5 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | LEU126-ALA147 | |
C | LEU126-ALA147 |
site_id | SWS_FT_FI6 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | ASN167-PHE188 | |
C | ASN167-PHE188 |
site_id | SWS_FT_FI7 |
Number of Residues | 44 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | PHE215-TYR237 | |
C | PHE215-TYR237 |
site_id | SWS_FT_FI8 |
Number of Residues | 46 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | LEU261-LEU284 | |
C | LEU261-LEU284 |
site_id | SWS_FT_FI9 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=7 => ECO:0000269|PubMed:25822790 |
Chain | Residue | Details |
A | ALA304-PHE325 | |
C | ALA304-PHE325 |
site_id | SWS_FT_FI10 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000305|PubMed:25822790, ECO:0007744|PDB:4XNW |
Chain | Residue | Details |
A | LYS46 | |
C | ARG310 | |
A | TYR203 | |
A | ASN283 | |
A | TYR303 | |
A | ARG310 | |
C | LYS46 | |
C | TYR203 | |
C | ASN283 | |
C | TYR303 |
site_id | SWS_FT_FI11 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN11 | |
A | ASN27 | |
A | ASN113 | |
A | ASN197 | |
C | ASN11 | |
C | ASN27 | |
C | ASN113 | |
C | ASN197 |
site_id | SWS_FT_FI12 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00241, ECO:0000269|PubMed:10216292 |
Chain | Residue | Details |
A | CYS1006 | |
A | CYS1009 | |
A | CYS1039 | |
A | CYS1042 | |
C | CYS1006 | |
C | CYS1009 | |
C | CYS1039 | |
C | CYS1042 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: N-formylmethionine => ECO:0000269|PubMed:1637309 |
Chain | Residue | Details |
A | MET1001 | |
C | MET1001 |