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7UL3

CryoEM Structure of Inactive H2R Bound to Famotidine, Nb6M, and NabFab

Functional Information from GO Data
ChainGOidnamespacecontents
A0001696biological_processgastric acid secretion
A0004930molecular_functionG protein-coupled receptor activity
A0004969molecular_functionhistamine receptor activity
A0007186biological_processG protein-coupled receptor signaling pathway
A0016020cellular_componentmembrane
A0045907biological_processpositive regulation of vasoconstriction
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIlNLFMISLDRYCaV
ChainResidueDetails
AALA104-VAL120

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR192-HIS198
HTYR194-HIS200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI2
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues23
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues27
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"38418462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Essential for histamine binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Essential for tiotidine binding and implicated in H2 selectivity","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Implicated in histamine binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues26
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails

248636

PDB entries from 2026-02-04

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