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5GLH

Human endothelin receptor type-B in complex with ET-1

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
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016998biological_processcell wall macromolecule catabolic process
A0030430cellular_componenthost cell cytoplasm
A0031640biological_processkilling of cells of another organism
A0042742biological_processdefense response to bacterium
A0044659biological_processviral release from host cell by cytolysis
B0005576cellular_componentextracellular region
B0019229biological_processregulation of vasoconstriction
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

site_idPS00270
Number of Residues15
DetailsENDOTHELIN Endothelin family signature. CsCsslmDkeCvyFC
ChainResidueDetails
BCYS1-CYS15

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsTRANSMEM: Helical; Name=1 => ECO:0000255
ChainResidueDetails
ATYR102-ILE126

site_idSWS_FT_FI2
Number of Residues30
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
ATYR127-ASN137
AASP198-THR218

site_idSWS_FT_FI3
Number of Residues25
DetailsTRANSMEM: Helical; Name=2 => ECO:0000255
ChainResidueDetails
AILE138-LEU163

site_idSWS_FT_FI4
Number of Residues49
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
AALA164-LYS175
ATHR244-THR271
AASN351-SER362

site_idSWS_FT_FI5
Number of Residues21
DetailsTRANSMEM: Helical; Name=3 => ECO:0000255
ChainResidueDetails
ALEU176-ILE197

site_idSWS_FT_FI6
Number of Residues24
DetailsTRANSMEM: Helical; Name=4 => ECO:0000255
ChainResidueDetails
AALA219-ILE243

site_idSWS_FT_FI7
Number of Residues24
DetailsTRANSMEM: Helical; Name=5 => ECO:0000255
ChainResidueDetails
AALA272-MET296

site_idSWS_FT_FI8
Number of Residues25
DetailsTRANSMEM: Helical; Name=6 => ECO:0000255
ChainResidueDetails
AVAL325-TYR350

site_idSWS_FT_FI9
Number of Residues26
DetailsTRANSMEM: Helical; Name=7 => ECO:0000255
ChainResidueDetails
APHE363-VAL389

site_idSWS_FT_FI10
Number of Residues1
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:9261180
ChainResidueDetails
ACYS402

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000255
ChainResidueDetails
ACYS403
AALA405

site_idSWS_FT_FI12
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AGLU1011

site_idSWS_FT_FI13
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
ChainResidueDetails
AASP1020

site_idSWS_FT_FI14
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:8266098
ChainResidueDetails
ALEU1032
APHE1104

site_idSWS_FT_FI15
Number of Residues2
DetailsBINDING: BINDING => ECO:0000303|PubMed:7831309
ChainResidueDetails
ASER1117
AASN1132

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 921
ChainResidueDetails
AGLU1011proton shuttle (general acid/base)
AASP1020covalent catalysis

226707

PDB entries from 2024-10-30

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