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5XPR

Human endothelin receptor type-B in complex with antagonist bosentan

Functional Information from GO Data
ChainGOidnamespacecontents
A0003796molecular_functionlysozyme activity
A0004930molecular_functionG protein-coupled receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0016998biological_processcell wall macromolecule catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue K86 A 1201
ChainResidue
AASP154
ATRP336
ALEU339
AHIS340
AARG343
AILE372
APRO178
AGLN181
ALYS182
AVAL185
ACYS255
ALYS273
ALEU277
ATYR281

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 1202
ChainResidue
AVAL203
ATRP206
ASER207
ALYS303
AARG318

site_idAC3
Number of Residues5
Detailsbinding site for residue SO4 A 1203
ChainResidue
APRO136
AASN137
AARG199
AGLN317
AARG1094

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 1204
ChainResidue
AARG208
AASN1073
AASN1089

site_idAC5
Number of Residues4
Detailsbinding site for residue SO4 A 1205
ChainResidue
ALYS216
ATHR1099
APRO1100
AASN1101

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_FI1
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8266098","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7831309","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues30
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues49
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P28088","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"9261180","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues
DetailsM-CSA 921
ChainResidueDetails

245663

PDB entries from 2025-12-03

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