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6CGB

chimera of mouse cadherin-11 EC1 and mouse cadherin-6 EC2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
A0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue CA A 301
ChainResidue
AGLU11
AGLU66
AASP98
AILE99
AASP101
AASN102
AASP134

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 302
ChainResidue
AASP64
AGLU66
AASP101
AGLU11
AGLU12

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AASN100
AASN102
AASP132
AASP134
ASER141
AASP187

site_idAC4
Number of Residues2
Detailsbinding site for residue GOL A 305
ChainResidue
AGLU12
AASP101

site_idAC5
Number of Residues1
Detailsbinding site for residue GOL A 306
ChainResidue
AASP32

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. VkVqDiNDNeP
ChainResidueDetails
AVAL94-PRO104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues105
DetailsDomain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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