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6IGL

Crystal Structure of human ETB receptor in complex with IRL1620

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0009253biological_processpeptidoglycan catabolic process
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
B0005576cellular_componentextracellular region
B0019229biological_processregulation of vasoconstriction
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue CIT A 1201
ChainResidue
AARG1006
AGLY1111
APHE1112
ATHR1113
AASN1114
ASER1115
AASN1130
AHOH1307
AHOH1333

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 1202
ChainResidue
ALYS303
AHIS314
AGLU1003
AARG1006
ALYS1058
AGLU1062
AHOH1301

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 A 1203
ChainResidue
AGLY1049
AARG1050
ALYS1058
AASP1059
ALYS1133
AHOH1303
AHOH1327

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 1204
ChainResidue
ATHR1140
APRO1141
AASN1142
AARG1143

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 1205
ChainResidue
ASER1036
ALEU1037
AASN1038

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 1206
ChainResidue
ATYR200
AARG201

site_idAC7
Number of Residues8
Detailsbinding site for residue OLC A 1207
ChainResidue
ASER1036
AASN1038
ALYS1122
AARG1123
ATRP1124
AASP1125
AGLU1126
AOLC1208

site_idAC8
Number of Residues6
Detailsbinding site for residue OLC A 1208
ChainResidue
AARG319
ALYS323
AARG1152
ATHR1153
ATHR1155
AOLC1207

Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ITVlSLCALSIDRYRaV
ChainResidueDetails
AILE187-VAL203

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues30
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues49
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28088","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"9261180","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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