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3Q2W

Crystal structure of mouse N-cadherin ectodomain

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
A0098609biological_processcell-cell adhesion
Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. InViDmNDNrP
ChainResidueDetails
AILE96-PRO106
AILE211-PRO221
AILE434-PRO444

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ
ChainResidueDetails
AGLU11
AASP194
AASP67
AGLU69
AASP100
AMET101
AASN102
AASN104
AASP136
AASN142

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21366346, ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ
ChainResidueDetails
AASP103
AASP134

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN31
AASN533

site_idSWS_FT_FI4
Number of Residues5
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21300292, ECO:0007744|PDB:3Q2W
ChainResidueDetails
AASN114
AASN166
AASN243
AASN413
AASN492

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PDB entries from 2024-05-01

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