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

7T4R

CryoEM structure of the HCMV Pentamer gH/gL/UL128/UL130/UL131A in complex with THBD and neutralizing fabs MSL-109 and 13H11

Functional Information from GO Data
ChainGOidnamespacecontents
A0004888molecular_functiontransmembrane signaling receptor activity
A0005509molecular_functioncalcium ion binding
A0016020cellular_componentmembrane
C0016032biological_processviral process
C0019031cellular_componentviral envelope
D0019031cellular_componentviral envelope
D0019062biological_processvirion attachment to host cell
D0044423cellular_componentvirion component
D0046718biological_processsymbiont entry into host cell
D0055036cellular_componentvirion membrane
D0098670biological_processentry receptor-mediated virion attachment to host cell
L0016032biological_processviral process
L0019031cellular_componentviral envelope
M0019031cellular_componentviral envelope
M0019062biological_processvirion attachment to host cell
M0044423cellular_componentvirion component
M0046718biological_processsymbiont entry into host cell
M0055036cellular_componentvirion membrane
M0098670biological_processentry receptor-mediated virion attachment to host cell
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtqggFeChC
ChainResidueDetails
ACYS340-CYS351
ACYS455-CYS466

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
GTYR204-HIS210
HTYR192-HIS198
ITYR220-HIS226
JTYR234-HIS240

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CmCetGYrlaadqhrC
ChainResidueDetails
ACYS308-CYS323
ACYS425-CYS439

site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvDDCilepsp........Cpqr....CvNtqggFeC
ChainResidueDetails
AASP325-CYS349
AASP441-CYS464

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues126
DetailsRegion: {"description":"Interaction with gL","evidences":[{"source":"HAMAP-Rule","id":"MF_04033","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04033","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues213
DetailsDomain: {"description":"gL betaherpesvirus-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01369","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

PDB entries from 2026-02-25

PDB statisticsPDBj update infoContact PDBjnumon