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6MGA

Crystal Structure of Human Protocadherin-1 EC1-4 with glycosylation

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
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeVqDiNDNtP
ChainResidueDetails
AILE99-PRO109
AVAL211-PRO221
AVAL318-PRO328

site_idPS00830
Number of Residues17
DetailsGREAB_2 Prokaryotic transcription elongation factors signature 2. SenSPIGhSVIqvkaND
ChainResidueDetails
ASER233-ASP249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN248

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN346

222926

PDB entries from 2024-07-24

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