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 | 106 |
| Details | Domain: {"description":"Rubredoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00241","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10216292","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-formylmethionine","evidences":[{"source":"PubMed","id":"1637309","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 60 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 116 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 44 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 46 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 42 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25822790","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4XNW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






