4NUQ

Crystal structure of mouse N-cadherin EC1-2 W2F

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005886	cellular_component	plasma membrane
A	0007155	biological_process	cell adhesion
A	0007156	biological_process	homophilic cell adhesion via plasma membrane adhesion molecules
A	0016020	cellular_component	membrane
A	0098609	biological_process	cell-cell adhesion

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 301

Chain	Residue
A	GLU11
A	ASP67
A	GLU69
A	ASP103
A	HOH413
A	HOH448

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 302

Chain	Residue
A	MET101
A	ASP103
A	ASP136
A	GLU11
A	GLU69
A	ASP100

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 303

Chain	Residue
A	ASN102
A	ASN104
A	ASP134
A	ASP136
A	ASN142
A	ASP194

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Functional Information from PROSITE/UniProt

site_id	PS00232
Number of Residues	11
Details	CADHERIN_1 Cadherin domain signature. InViDmNDNrP

Chain	Residue	Details
A	ILE96-PRO106

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	BINDING: BINDING => ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ

Chain	Residue	Details
A	GLU11
A	ASP194
A	ASP67
A	GLU69
A	ASP100
A	MET101
A	ASN102
A	ASN104
A	ASP136
A	ASN142

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:21366346, ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ

Chain	Residue	Details
A	ASP103
A	ASP134

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN31

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21300292, ECO:0007744|PDB:3Q2W

Chain	Residue	Details
A	ASN114
A	ASN166

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