Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7M93

Bovine sigma-2 receptor bound to PB28

Functional Information from GO Data
ChainGOidnamespacecontents
A0005764cellular_componentlysosome
A0005783cellular_componentendoplasmic reticulum
A0005791cellular_componentrough endoplasmic reticulum
A0005886cellular_componentplasma membrane
A0008142molecular_functionoxysterol binding
A0015485molecular_functioncholesterol binding
A0030867cellular_componentrough endoplasmic reticulum membrane
A0031965cellular_componentnuclear membrane
A0032377biological_processregulation of intracellular lipid transport
A0032383biological_processregulation of intracellular cholesterol transport
A0042632biological_processcholesterol homeostasis
A0090303biological_processpositive regulation of wound healing
A0140077biological_processpositive regulation of lipoprotein transport
B0005764cellular_componentlysosome
B0005783cellular_componentendoplasmic reticulum
B0005791cellular_componentrough endoplasmic reticulum
B0005886cellular_componentplasma membrane
B0008142molecular_functionoxysterol binding
B0015485molecular_functioncholesterol binding
B0030867cellular_componentrough endoplasmic reticulum membrane
B0031965cellular_componentnuclear membrane
B0032377biological_processregulation of intracellular lipid transport
B0032383biological_processregulation of intracellular cholesterol transport
B0042632biological_processcholesterol homeostasis
B0090303biological_processpositive regulation of wound healing
B0140077biological_processpositive regulation of lipoprotein transport
C0005764cellular_componentlysosome
C0005783cellular_componentendoplasmic reticulum
C0005791cellular_componentrough endoplasmic reticulum
C0005886cellular_componentplasma membrane
C0008142molecular_functionoxysterol binding
C0015485molecular_functioncholesterol binding
C0030867cellular_componentrough endoplasmic reticulum membrane
C0031965cellular_componentnuclear membrane
C0032377biological_processregulation of intracellular lipid transport
C0032383biological_processregulation of intracellular cholesterol transport
C0042632biological_processcholesterol homeostasis
C0090303biological_processpositive regulation of wound healing
C0140077biological_processpositive regulation of lipoprotein transport
D0005764cellular_componentlysosome
D0005783cellular_componentendoplasmic reticulum
D0005791cellular_componentrough endoplasmic reticulum
D0005886cellular_componentplasma membrane
D0008142molecular_functionoxysterol binding
D0015485molecular_functioncholesterol binding
D0030867cellular_componentrough endoplasmic reticulum membrane
D0031965cellular_componentnuclear membrane
D0032377biological_processregulation of intracellular lipid transport
D0032383biological_processregulation of intracellular cholesterol transport
D0042632biological_processcholesterol homeostasis
D0090303biological_processpositive regulation of wound healing
D0140077biological_processpositive regulation of lipoprotein transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue YT1 A 201
ChainResidue
AASP29
ATYR147
ATYR150

site_idAC2
Number of Residues3
Detailsbinding site for residue OLC A 202
ChainResidue
AALA6
AILE156
AOLC203

site_idAC3
Number of Residues4
Detailsbinding site for residue OLC A 203
ChainResidue
AOLC202
ALEU152
ALEU159
AARG163

site_idAC4
Number of Residues4
Detailsbinding site for residue OLC A 204
ChainResidue
AILE83
AOLC206
DLEU141
DSER145

site_idAC5
Number of Residues3
Detailsbinding site for residue OLC A 205
ChainResidue
ALEU19
ATYR86
APHE89

site_idAC6
Number of Residues5
Detailsbinding site for residue OLC A 206
ChainResidue
APHE80
APRO99
ATYR103
AHIS106
AOLC204

site_idAC7
Number of Residues4
Detailsbinding site for residue OLC A 207
ChainResidue
ATYR86
DLEU119
DPHE137
DARG140

site_idAC8
Number of Residues7
Detailsbinding site for residue YT1 B 201
ChainResidue
ALEU46
BILE24
BASP29
BTYR50
BLEU59
BTYR147
BTYR150

site_idAC9
Number of Residues3
Detailsbinding site for residue OLC B 202
ChainResidue
BPHE76
BILE83
BOLC203

site_idAD1
Number of Residues5
Detailsbinding site for residue OLC B 203
ChainResidue
BPHE76
BPRO99
BILE102
BHIS106
BOLC202

site_idAD2
Number of Residues4
Detailsbinding site for residue YT1 C 201
ChainResidue
CILE24
CASP29
CVAL146
CTYR147

site_idAD3
Number of Residues7
Detailsbinding site for residue OLC C 202
ChainResidue
BILE156
BARG163
CLEU26
CLEU34
CLEU38
CTYR39
CPRO40

site_idAD4
Number of Residues5
Detailsbinding site for residue OLC C 203
ChainResidue
CPHE80
CILE102
CTYR103
CHIS106
DTHR109

site_idAD5
Number of Residues3
Detailsbinding site for residue OLC C 204
ChainResidue
CLEU19
CPRO82
CTYR86

site_idAD6
Number of Residues5
Detailsbinding site for residue OLC C 205
ChainResidue
CSER116
CLEU120
CPHE151
DLYS67
DPHE71

site_idAD7
Number of Residues6
Detailsbinding site for residue YT1 D 201
ChainResidue
CGLU42
DASP29
DLEU59
DVAL146
DTYR147
DTYR150

site_idAD8
Number of Residues6
Detailsbinding site for residue OLC D 202
ChainResidue
CMET108
DPHE76
DPHE80
DPRO99
DILE102
DHIS106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues208
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"UniProtKB","id":"Q12155","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues36
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"Q12155","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues80
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues444
DetailsDomain: {"description":"EXPERA","evidences":[{"source":"PROSITE-ProRule","id":"PRU01087","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34880501","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7MFI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsSite: {"description":"Likely important for receptor folding","evidences":[{"source":"UniProtKB","id":"Q5BJF2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Important for 20(S)-OHC binding and stereoselectivity","evidences":[{"source":"UniProtKB","id":"Q5BJF2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon