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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7A7D

Cadherin fit into cryo-ET map

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0016020cellular_componentmembrane
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
C0016020cellular_componentmembrane
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
F0005509molecular_functioncalcium ion binding
F0005886cellular_componentplasma membrane
F0007155biological_processcell adhesion
F0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
F0016020cellular_componentmembrane
G0005509molecular_functioncalcium ion binding
G0005886cellular_componentplasma membrane
G0007155biological_processcell adhesion
G0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
G0016020cellular_componentmembrane
a0005509molecular_functioncalcium ion binding
a0005886cellular_componentplasma membrane
a0007155biological_processcell adhesion
a0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
a0016020cellular_componentmembrane
b0005509molecular_functioncalcium ion binding
b0005886cellular_componentplasma membrane
b0007155biological_processcell adhesion
b0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
b0016020cellular_componentmembrane
c0005509molecular_functioncalcium ion binding
c0005886cellular_componentplasma membrane
c0007155biological_processcell adhesion
c0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
c0016020cellular_componentmembrane
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
f0005509molecular_functioncalcium ion binding
f0005886cellular_componentplasma membrane
f0007155biological_processcell adhesion
f0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
f0016020cellular_componentmembrane
g0005509molecular_functioncalcium ion binding
g0005886cellular_componentplasma membrane
g0007155biological_processcell adhesion
g0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
g0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IkIeDeNDNyP
ChainResidueDetails
aILE2360-PRO2370
aILE2472-PRO2482
aILE2694-PRO2704
AILE98-PRO108
AILE211-PRO221
AILE438-PRO448
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1519
DetailsDomain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1561
DetailsDomain: {"description":"Cadherin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1603
DetailsDomain: {"description":"Cadherin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1547
DetailsDomain: {"description":"Cadherin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12754519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues21
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-08-13

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