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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9CLI

Cryo-EM model derived from localized reconstruction of human adenovirus (Ad5)-hexon-FX complex at 3.6A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
J0005198molecular_functionstructural molecule activity
J0019028cellular_componentviral capsid
J0039623cellular_componentT=25 icosahedral viral capsid
J0042025cellular_componenthost cell nucleus
J0043657cellular_componenthost cell
J0044423cellular_componentvirion component
J0046718biological_processsymbiont entry into host cell
J0075521biological_processmicrotubule-dependent intracellular transport of viral material towards nucleus
J0075606biological_processtransport of viral material towards nucleus
K0005198molecular_functionstructural molecule activity
K0019028cellular_componentviral capsid
K0039623cellular_componentT=25 icosahedral viral capsid
K0042025cellular_componenthost cell nucleus
K0043657cellular_componenthost cell
K0044423cellular_componentvirion component
K0046718biological_processsymbiont entry into host cell
K0075521biological_processmicrotubule-dependent intracellular transport of viral material towards nucleus
K0075606biological_processtransport of viral material towards nucleus
L0005198molecular_functionstructural molecule activity
L0019028cellular_componentviral capsid
L0039623cellular_componentT=25 icosahedral viral capsid
L0042025cellular_componenthost cell nucleus
L0043657cellular_componenthost cell
L0044423cellular_componentvirion component
L0046718biological_processsymbiont entry into host cell
L0075521biological_processmicrotubule-dependent intracellular transport of viral material towards nucleus
L0075606biological_processtransport of viral material towards nucleus
Z0004252molecular_functionserine-type endopeptidase activity
Z0005509molecular_functioncalcium ion binding
Z0005576cellular_componentextracellular region
Z0006508biological_processproteolysis
Z0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
ZCYS61-CYS72
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
ZCGU16-TRP41
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
ZCYS70-CYS81
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
ZLEU232-CYS237
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV
ChainResidueDetails
ZASP373-VAL384
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
ZCYS70-CYS81
ZCYS109-CYS124
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
ZASP46-CYS70
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSite: {"description":"Involved in interaction with pre-protein VI","evidences":[{"source":"HAMAP-Rule","id":"MF_04051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04051","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues11
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GalNAc...) threonine","evidences":[{"source":"PubMed","id":"8243461","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000012","evidences":[{"source":"PubMed","id":"8243461","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000013","evidences":[{"source":"PubMed","id":"8243461","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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