6OAE

Crystal Structure of Human Mucin-like Protocadherin EC1-2

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	7
Details	binding site for residue TRS A 301

Chain	Residue
A	VAL7
A	VAL7
A	ASN8
A	ASN8
A	ASP10
A	ASP10
A	HOH423

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 302

Chain	Residue
A	ASP91
A	VAL92
A	ASP94
A	ASP130
A	GLU16
A	GLU62

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 303

Chain	Residue
A	GLU16
A	ASP60
A	GLU62
A	ASP94
A	HOH435
A	HOH498

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA A 304

Chain	Residue
A	ASN93
A	ASN95
A	ASP128
A	ASP130
A	ASP133
A	ASP182

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL87-PRO97

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	53
Details	Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---