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8XQJ

Cryo-EM structure of human dimeric APJR complex with antagonistic antibody

Functional Information from GO Data
ChainGOidnamespacecontents
C0004930molecular_functionG protein-coupled receptor activity
C0005506molecular_functioniron ion binding
C0007186biological_processG protein-coupled receptor signaling pathway
C0009055molecular_functionelectron transfer activity
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0022900biological_processelectron transport chain
C0042597cellular_componentperiplasmic space
D0004930molecular_functionG protein-coupled receptor activity
D0005506molecular_functioniron ion binding
D0007186biological_processG protein-coupled receptor signaling pathway
D0009055molecular_functionelectron transfer activity
D0016020cellular_componentmembrane
D0020037molecular_functionheme binding
D0022900biological_processelectron transport chain
D0042597cellular_componentperiplasmic space
Functional Information from PROSITE/UniProt
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASVfCLTGLSFDRYLaI
ChainResidueDetails
CALA115-ILE131

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=1","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues102
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues126
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsTransmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues48
DetailsTransmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=6","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues44
DetailsTransmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7W0O","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Required for APELA and APLN/apelin-13 interaction and signaling","evidences":[{"source":"PubMed","id":"35817871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"38428423","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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