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

7BR3

Crystal structure of the protein 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016500molecular_functionprotein-hormone receptor activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue OLC A 1202
ChainResidue
ASER34

site_idAC2
Number of Residues2
Detailsbinding site for residue OLC A 1203
ChainResidue
ALEU58
AASP293

site_idAC3
Number of Residues3
Detailsbinding site for residue PEG A 1204
ChainResidue
ALEU33
ASER140
ALEU141

site_idAC4
Number of Residues2
Detailsbinding site for residue PEG A 1205
ChainResidue
AILE37
AILE226

site_idAC5
Number of Residues1
Detailsbinding site for residue PEG A 1206
ChainResidue
APHE130

site_idAC6
Number of Residues4
Detailsbinding site for residue PEG A 1207
ChainResidue
ALEU300
AGLU1009
ALEU1012
AGLY1014

site_idAC7
Number of Residues5
Detailsbinding site for residue PEG A 1208
ChainResidue
AASN19
APHE52
ASER55
ATRP291
APHE292

site_idAC8
Number of Residues3
Detailsbinding site for residue PEG A 1209
ChainResidue
ATRP1007
AARG1102
AGLU1130

site_idAC9
Number of Residues2
Detailsbinding site for residue FMT A 1210
ChainResidue
AGLU1066
ALEU1174

site_idAD1
Number of Residues16
Detailsbinding site for residue F5O A 1211
ChainResidue
AILE21
APRO22
ALEU23
AGLN25
AGLY26
AASP98
AASN102
ALYS121
ATHR215
APHE216
ALEU219
ATYR283
ALEU286
AGLY287
ALEU297
AASN305

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues22
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

245663

PDB entries from 2025-12-03

PDB statisticsPDBj update infoContact PDBjnumon