7M94
Bovine sigma-2 receptor bound to Roluperidone
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005764 | cellular_component | lysosome |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008142 | molecular_function | oxysterol binding |
| A | 0015485 | molecular_function | cholesterol binding |
| A | 0030867 | cellular_component | rough endoplasmic reticulum membrane |
| A | 0031965 | cellular_component | nuclear membrane |
| A | 0032377 | biological_process | regulation of intracellular lipid transport |
| A | 0032383 | biological_process | regulation of intracellular cholesterol transport |
| A | 0042632 | biological_process | cholesterol homeostasis |
| A | 0090303 | biological_process | positive regulation of wound healing |
| A | 0140077 | biological_process | positive regulation of lipoprotein transport |
| B | 0005764 | cellular_component | lysosome |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005791 | cellular_component | rough endoplasmic reticulum |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008142 | molecular_function | oxysterol binding |
| B | 0015485 | molecular_function | cholesterol binding |
| B | 0030867 | cellular_component | rough endoplasmic reticulum membrane |
| B | 0031965 | cellular_component | nuclear membrane |
| B | 0032377 | biological_process | regulation of intracellular lipid transport |
| B | 0032383 | biological_process | regulation of intracellular cholesterol transport |
| B | 0042632 | biological_process | cholesterol homeostasis |
| B | 0090303 | biological_process | positive regulation of wound healing |
| B | 0140077 | biological_process | positive regulation of lipoprotein transport |
| C | 0005764 | cellular_component | lysosome |
| C | 0005783 | cellular_component | endoplasmic reticulum |
| C | 0005791 | cellular_component | rough endoplasmic reticulum |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0008142 | molecular_function | oxysterol binding |
| C | 0015485 | molecular_function | cholesterol binding |
| C | 0030867 | cellular_component | rough endoplasmic reticulum membrane |
| C | 0031965 | cellular_component | nuclear membrane |
| C | 0032377 | biological_process | regulation of intracellular lipid transport |
| C | 0032383 | biological_process | regulation of intracellular cholesterol transport |
| C | 0042632 | biological_process | cholesterol homeostasis |
| C | 0090303 | biological_process | positive regulation of wound healing |
| C | 0140077 | biological_process | positive regulation of lipoprotein transport |
| D | 0005764 | cellular_component | lysosome |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005791 | cellular_component | rough endoplasmic reticulum |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008142 | molecular_function | oxysterol binding |
| D | 0015485 | molecular_function | cholesterol binding |
| D | 0030867 | cellular_component | rough endoplasmic reticulum membrane |
| D | 0031965 | cellular_component | nuclear membrane |
| D | 0032377 | biological_process | regulation of intracellular lipid transport |
| D | 0032383 | biological_process | regulation of intracellular cholesterol transport |
| D | 0042632 | biological_process | cholesterol homeostasis |
| D | 0090303 | biological_process | positive regulation of wound healing |
| D | 0140077 | biological_process | positive regulation of lipoprotein transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue YT7 A 201 |
| Chain | Residue |
| A | MET28 |
| A | ASP29 |
| A | GLN47 |
| A | GLU73 |
| A | GLN77 |
| A | THR107 |
| A | THR110 |
| A | TYR147 |
| A | TYR150 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue OLC A 202 |
| Chain | Residue |
| A | PHE76 |
| A | HIS106 |
| B | MET108 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue OLC A 203 |
| Chain | Residue |
| A | SER116 |
| A | PHE151 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue OLC A 204 |
| Chain | Residue |
| A | PHE71 |
| B | LEU120 |
| B | OLC205 |
| D | THR3 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue OLC A 205 |
| Chain | Residue |
| A | SER116 |
| A | LEU120 |
| B | LYS67 |
| B | SER68 |
| B | PHE71 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue YT7 B 201 |
| Chain | Residue |
| B | ILE24 |
| B | MET28 |
| B | ASP29 |
| B | TYR50 |
| B | GLU73 |
| B | GLN77 |
| B | THR110 |
| B | VAL146 |
| B | TYR147 |
| B | TYR150 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue OLC B 203 |
| Chain | Residue |
| B | OLC209 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue OLC B 204 |
| Chain | Residue |
| B | LEU27 |
| B | MET28 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue OLC B 205 |
| Chain | Residue |
| A | OLC204 |
| B | SER116 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue OLC B 206 |
| Chain | Residue |
| B | LEU119 |
| B | PHE137 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue OLC B 207 |
| Chain | Residue |
| B | THR3 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 208 |
| Chain | Residue |
| B | LEU26 |
| B | LEU38 |
| B | PRO40 |
| B | LEU74 |
| B | PRO79 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue OLC B 209 |
| Chain | Residue |
| A | VAL162 |
| B | PHE76 |
| B | ILE102 |
| B | HIS106 |
| B | OLC203 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue YT7 C 201 |
| Chain | Residue |
| C | HIS21 |
| C | MET28 |
| C | ASP29 |
| C | GLU73 |
| C | GLN77 |
| C | THR107 |
| C | VAL146 |
| C | TYR147 |
| C | TYR150 |
| C | HOH302 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC C 202 |
| Chain | Residue |
| C | PHE76 |
| C | PRO99 |
| C | HIS106 |
| C | OLC203 |
| D | THR109 |
| site_id | AD7 |
| Number of Residues | 1 |
| Details | binding site for residue OLC C 203 |
| Chain | Residue |
| C | OLC202 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue OLC C 204 |
| Chain | Residue |
| C | LEU34 |
| C | LEU38 |
| C | TYR39 |
| C | PRO40 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue OLC C 205 |
| Chain | Residue |
| C | LYS67 |
| D | LEU120 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue OLC C 206 |
| Chain | Residue |
| C | SER116 |
| C | LEU120 |
| C | ASP121 |
| D | ALA64 |
| D | LYS67 |
| D | SER68 |
| D | PHE71 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue YT7 D 201 |
| Chain | Residue |
| D | MET28 |
| D | ASP29 |
| D | GLU73 |
| D | GLN77 |
| D | THR110 |
| D | VAL146 |
| D | TYR147 |
| D | TYR150 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue OLC D 202 |
| Chain | Residue |
| D | LEU38 |
| D | TYR39 |
| D | LEU74 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue OLC D 203 |
| Chain | Residue |
| D | VAL162 |
| D | ARG163 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue OLC D 204 |
| Chain | Residue |
| D | PHE80 |
| D | PRO99 |
| D | ILE102 |
| D | HIS106 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue OLC D 205 |
| Chain | Residue |
| D | GLY5 |
| D | LEU10 |
| D | ILE156 |
| A | PHE71 |
| D | THR3 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 208 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"UniProtKB","id":"Q12155","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"Q12155","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34880501","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MFI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Site: {"description":"Likely important for receptor folding","evidences":[{"source":"UniProtKB","id":"Q5BJF2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for 20(S)-OHC binding and stereoselectivity","evidences":[{"source":"UniProtKB","id":"Q5BJF2","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 444 |
| Details | Domain: {"description":"EXPERA","evidences":[{"source":"PROSITE-ProRule","id":"PRU01087","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
