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8QJX

Human Adenovirus type 11 fiber knob in complex with two copies of its cell receptor, Desmoglein-2

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0019028cellular_componentviral capsid
A0019058biological_processviral life cycle
A0019062biological_processvirion attachment to host cell
A0042025cellular_componenthost cell nucleus
A0046718biological_processsymbiont entry into host cell
A0098671biological_processadhesion receptor-mediated virion attachment to host cell
B0007155biological_processcell adhesion
B0019028cellular_componentviral capsid
B0019058biological_processviral life cycle
B0019062biological_processvirion attachment to host cell
B0042025cellular_componenthost cell nucleus
B0046718biological_processsymbiont entry into host cell
B0098671biological_processadhesion receptor-mediated virion attachment to host cell
C0007155biological_processcell adhesion
C0019028cellular_componentviral capsid
C0019058biological_processviral life cycle
C0019062biological_processvirion attachment to host cell
C0042025cellular_componenthost cell nucleus
C0046718biological_processsymbiont entry into host cell
C0098671biological_processadhesion receptor-mediated virion attachment to host cell
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
D0016020cellular_componentmembrane
E0005509molecular_functioncalcium ion binding
E0005886cellular_componentplasma membrane
E0007155biological_processcell adhesion
E0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
E0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IkVlDiNDNeP
ChainResidueDetails
DILE98-PRO108
DILE211-PRO221
DILE438-PRO448

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1118
DetailsTOPO_DOM: Extracellular => ECO:0000255
ChainResidueDetails
DALA1-GLY560
EALA1-GLY560

site_idSWS_FT_FI2
Number of Residues48
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
DLEU561-MET585
ELEU561-MET585

site_idSWS_FT_FI3
Number of Residues966
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
DCYS586-SER1069
ECYS586-SER1069

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER631
ESER631

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER651
DSER757
DSER761
DSER766
ESER651
ESER757
ESER761
ESER766

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692
ChainResidueDetails
DSER654
ESER654

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER674
DSER677
ESER674
ESER677

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
DTHR755
DTHR873
ETHR755
ETHR873

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
DSER1069
ESER1069

site_idSWS_FT_FI10
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218
ChainResidueDetails
DASN63
EASN63

site_idSWS_FT_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973
ChainResidueDetails
DASN133
EASN133

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
DASN260
DASN465
EASN260
EASN465

site_idSWS_FT_FI13
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19349973
ChainResidueDetails
DASN413
EASN413

219869

PDB entries from 2024-05-15

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