4RWD
XFEL structure of the human delta opioid receptor in complex with a bifunctional peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004930 | molecular_function | G protein-coupled receptor activity |
| A | 0004985 | molecular_function | G protein-coupled opioid 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 | 0016020 | cellular_component | membrane |
| A | 0020037 | molecular_function | heme binding |
| A | 0022900 | biological_process | electron transport chain |
| A | 0038046 | molecular_function | G protein-coupled enkephalin receptor activity |
| A | 0042597 | cellular_component | periplasmic space |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004930 | molecular_function | G protein-coupled receptor activity |
| B | 0004985 | molecular_function | G protein-coupled opioid receptor activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0016020 | cellular_component | membrane |
| B | 0020037 | molecular_function | heme binding |
| B | 0022900 | biological_process | electron transport chain |
| B | 0038046 | molecular_function | G protein-coupled enkephalin receptor activity |
| B | 0042597 | cellular_component | periplasmic space |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE OLA A 1201 |
| Chain | Residue |
| A | ILE50 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1202 |
| Chain | Residue |
| A | ASP95 |
| A | ASN131 |
| A | SER135 |
| A | HOH1309 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 1204 |
| Chain | Residue |
| A | LYS81 |
| A | ILE86 |
| A | LEU93 |
| A | ASN169 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE OLC A 1205 |
| Chain | Residue |
| A | MET141 |
| A | ILE168 |
| A | ILE172 |
| A | LEU175 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLA A 1206 |
| Chain | Residue |
| A | SER44 |
| A | PRO294 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLA B 1201 |
| Chain | Residue |
| B | SER44 |
| B | OLA1204 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 1202 |
| Chain | Residue |
| B | ASP95 |
| B | ASN131 |
| B | SER135 |
| B | HOH1313 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE OLA B 1204 |
| Chain | Residue |
| B | LEU48 |
| B | OLA1201 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE OLC B 1205 |
| Chain | Residue |
| B | ILE86 |
| B | PHE89 |
| B | TRP173 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN G OF BIFUNCTIONAL PEPTIDE |
| Chain | Residue |
| B | ASP128 |
| B | TYR129 |
| B | MET132 |
| B | MET199 |
| B | LEU200 |
| B | LYS214 |
| B | VAL217 |
| B | ILE277 |
| B | VAL281 |
| B | ILE304 |
| B | TYR308 |
| G | HOH101 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN H OF BIFUNCTIONAL PEPTIDE |
| Chain | Residue |
| A | ASP128 |
| A | TYR129 |
| A | MET132 |
| A | MET199 |
| A | LEU200 |
| A | LYS214 |
| A | VAL217 |
| A | ILE277 |
| A | VAL281 |
| A | ILE304 |
| A | TYR308 |
| H | HOH101 |
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. TSIfTLTMMSVDRYIaV |
| Chain | Residue | Details |
| A | THR134-VAL150 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: axial binding residue |
| Chain | Residue | Details |
| A | TRP1007 | |
| A | ILE1102 | |
| B | TRP1007 | |
| B | ILE1102 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 54 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU48-VAL75 | |
| B | LEU48-VAL75 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 98 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG76-ASN85 | |
| A | ASP145-ALA163 | |
| A | ARG239-ARG261 | |
| B | ARG76-ASN85 | |
| B | ASP145-ALA163 | |
| B | ARG239-ARG261 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 48 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000250 |
| Chain | Residue | Details |
| A | ILE86-LEU110 | |
| B | ILE86-LEU110 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 88 |
| Details | TOPO_DOM: Extracellular => ECO:0000250 |
| Chain | Residue | Details |
| A | MET111-LYS122 | |
| A | ALA187-SER206 | |
| A | THR285-ALA299 | |
| B | MET111-LYS122 | |
| B | ALA187-SER206 | |
| B | THR285-ALA299 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000250 |
| Chain | Residue | Details |
| A | ALA123-VAL144 | |
| B | ALA123-VAL144 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000250 |
| Chain | Residue | Details |
| A | LYS164-MET186 | |
| B | LYS164-MET186 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 62 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP207-LEU238 | |
| B | TRP207-LEU238 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 44 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000250 |
| Chain | Residue | Details |
| A | MET262-TRP284 | |
| B | MET262-TRP284 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 42 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU300-LEU321 | |
| B | LEU300-LEU321 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000255 |
| Chain | Residue | Details |
| A | CYS333 | |
| B | CYS333 |
