3LNE

Crystal structure of E-cadherin EC12 K14E

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-cell adhesion
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	GLU69
A	ASP100
A	GLN101
A	ASP103
A	ASP136

---

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

Chain	Residue
A	ASP136
A	ASN143
A	ASP195
A	ASN102
A	ASN104
A	ASP134

---

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

Chain	Residue
A	GLU11
A	ASP67
A	GLU69
A	ASP103
A	HOH269
A	HOH345

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 214

Chain	Residue
A	HIS159
A	LYS160
A	ASN161

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE96-PRO106

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	107
Details	Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"28973932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"28973932","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---