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7N86

Crystal Structure of Human Protocadherin-24 EC1-2 Form II

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell-cell adhesion
B0016020cellular_componentmembrane
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell-cell adhesion
C0016020cellular_componentmembrane
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007156biological_processhomophilic cell-cell adhesion
D0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. ViVeDrNDNaP
ChainResidueDetails
AVAL92-PRO102

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues388
DetailsDomain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues19
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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