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4XHZ

Crystal Structure of Human Protocadherin-15 EC8-10

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
A0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 2001
ChainResidue
AASN899
ATYR901
AASP931
AASP933
AALA939
AASP989

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 2002
ChainResidue
AMET898
AASP900
AGLU809
AGLU862
AASP897

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 2003
ChainResidue
AGLU809
AASP860
AGLU862
AASP900
AHOH2168

site_idAC4
Number of Residues3
Detailsbinding site for residue CL A 2004
ChainResidue
AVAL946
AVAL960
AARG970

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues106
DetailsDomain: {"description":"Cadherin 8","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsDomain: {"description":"Cadherin 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues107
DetailsDomain: {"description":"Cadherin 10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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