7M93
Bovine sigma-2 receptor bound to PB28
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
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 | 0016020 | cellular_component | membrane |
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 | 0005634 | cellular_component | nucleus |
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 | 0016020 | cellular_component | membrane |
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 | 0005634 | cellular_component | nucleus |
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 | 0016020 | cellular_component | membrane |
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 | 0005634 | cellular_component | nucleus |
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 | 0016020 | cellular_component | membrane |
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 | 3 |
Details | binding site for residue YT1 A 201 |
Chain | Residue |
A | ASP29 |
A | TYR147 |
A | TYR150 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue OLC A 202 |
Chain | Residue |
A | ALA6 |
A | ILE156 |
A | OLC203 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue OLC A 203 |
Chain | Residue |
A | OLC202 |
A | LEU152 |
A | LEU159 |
A | ARG163 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue OLC A 204 |
Chain | Residue |
A | ILE83 |
A | OLC206 |
D | LEU141 |
D | SER145 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue OLC A 205 |
Chain | Residue |
A | LEU19 |
A | TYR86 |
A | PHE89 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue OLC A 206 |
Chain | Residue |
A | PHE80 |
A | PRO99 |
A | TYR103 |
A | HIS106 |
A | OLC204 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue OLC A 207 |
Chain | Residue |
A | TYR86 |
D | LEU119 |
D | PHE137 |
D | ARG140 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue YT1 B 201 |
Chain | Residue |
A | LEU46 |
B | ILE24 |
B | ASP29 |
B | TYR50 |
B | LEU59 |
B | TYR147 |
B | TYR150 |
site_id | AC9 |
Number of Residues | 3 |
Details | binding site for residue OLC B 202 |
Chain | Residue |
B | PHE76 |
B | ILE83 |
B | OLC203 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue OLC B 203 |
Chain | Residue |
B | PHE76 |
B | PRO99 |
B | ILE102 |
B | HIS106 |
B | OLC202 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue YT1 C 201 |
Chain | Residue |
C | ILE24 |
C | ASP29 |
C | VAL146 |
C | TYR147 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue OLC C 202 |
Chain | Residue |
B | ILE156 |
B | ARG163 |
C | LEU26 |
C | LEU34 |
C | LEU38 |
C | TYR39 |
C | PRO40 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue OLC C 203 |
Chain | Residue |
C | PHE80 |
C | ILE102 |
C | TYR103 |
C | HIS106 |
D | THR109 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue OLC C 204 |
Chain | Residue |
C | LEU19 |
C | PRO82 |
C | TYR86 |
site_id | AD6 |
Number of Residues | 5 |
Details | binding site for residue OLC C 205 |
Chain | Residue |
C | SER116 |
C | LEU120 |
C | PHE151 |
D | LYS67 |
D | PHE71 |
site_id | AD7 |
Number of Residues | 6 |
Details | binding site for residue YT1 D 201 |
Chain | Residue |
C | GLU42 |
D | ASP29 |
D | LEU59 |
D | VAL146 |
D | TYR147 |
D | TYR150 |
site_id | AD8 |
Number of Residues | 6 |
Details | binding site for residue OLC D 202 |
Chain | Residue |
C | MET108 |
D | PHE76 |
D | PHE80 |
D | PRO99 |
D | ILE102 |
D | HIS106 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 68 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:Q12155 |
Chain | Residue | Details |
A | MET1-GLY9 | |
A | LYS90-PRO99 | |
B | MET1-GLY9 | |
B | LYS90-PRO99 | |
C | MET1-GLY9 | |
C | LYS90-PRO99 | |
D | MET1-GLY9 | |
D | LYS90-PRO99 |
site_id | SWS_FT_FI2 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
Chain | Residue | Details |
A | LEU10-LEU30 | |
B | LEU10-LEU30 | |
C | LEU10-LEU30 | |
D | LEU10-LEU30 |
site_id | SWS_FT_FI3 |
Number of Residues | 228 |
Details | TOPO_DOM: Lumenal => ECO:0000250|UniProtKB:Q12155 |
Chain | Residue | Details |
A | GLN31-SER68 | |
A | ASP121-LEU141 | |
B | GLN31-SER68 | |
B | ASP121-LEU141 | |
C | GLN31-SER68 | |
C | ASP121-LEU141 | |
D | GLN31-SER68 | |
D | ASP121-LEU141 |
site_id | SWS_FT_FI4 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
Chain | Residue | Details |
A | PHE69-PHE89 | |
B | PHE69-PHE89 | |
C | PHE69-PHE89 | |
D | PHE69-PHE89 |
site_id | SWS_FT_FI5 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
Chain | Residue | Details |
A | ALA100-LEU120 | |
B | ALA100-LEU120 | |
C | ALA100-LEU120 | |
D | ALA100-LEU120 |
site_id | SWS_FT_FI6 |
Number of Residues | 80 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
Chain | Residue | Details |
A | PHE142-VAL162 | |
B | PHE142-VAL162 | |
C | PHE142-VAL162 | |
D | PHE142-VAL162 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:34880501, ECO:0007744|PDB:7MFI |
Chain | Residue | Details |
A | VAL75 | |
A | GLN77 | |
B | VAL75 | |
B | GLN77 | |
C | VAL75 | |
C | GLN77 | |
D | VAL75 | |
D | GLN77 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | SITE: Likely important for receptor folding => ECO:0000250|UniProtKB:Q5BJF2 |
Chain | Residue | Details |
A | ASP56 | |
B | ASP56 | |
C | ASP56 | |
D | ASP56 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | SITE: Important for 20(S)-OHC binding and stereoselectivity => ECO:0000250|UniProtKB:Q5BJF2 |
Chain | Residue | Details |
A | TYR150 | |
B | TYR150 | |
C | TYR150 | |
D | TYR150 |