Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6PDL

Crystal Structure of Hendra Virus Attachment G Glycoprotein in Complex with Receptor Ephrin-B2

Functional Information from GO Data
ChainGOidnamespacecontents
A0019031cellular_componentviral envelope
A0019058biological_processviral life cycle
A0046789molecular_functionhost cell surface receptor binding
B0016020cellular_componentmembrane
B0046875molecular_functionephrin receptor binding
B0048013biological_processephrin receptor signaling pathway
C0019031cellular_componentviral envelope
C0019058biological_processviral life cycle
C0046789molecular_functionhost cell surface receptor binding
D0016020cellular_componentmembrane
D0046875molecular_functionephrin receptor binding
D0048013biological_processephrin receptor signaling pathway
E0019031cellular_componentviral envelope
E0019058biological_processviral life cycle
E0046789molecular_functionhost cell surface receptor binding
F0016020cellular_componentmembrane
F0046875molecular_functionephrin receptor binding
F0048013biological_processephrin receptor signaling pathway
G0019031cellular_componentviral envelope
G0019058biological_processviral life cycle
G0046789molecular_functionhost cell surface receptor binding
H0016020cellular_componentmembrane
H0046875molecular_functionephrin receptor binding
H0048013biological_processephrin receptor signaling pathway
Functional Information from PROSITE/UniProt
site_idPS01299
Number of Residues28
DetailsEPHRIN_RBD_1 Ephrin receptor-binding (ephrin RBD) domain signature. KFTiKFQeFSPnlwGlEFqknkdYYiiS
ChainResidueDetails
BLYS109-SER136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18488039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19836338","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

PDB statisticsPDBj update infoContact PDBjnumon