5KJ4

Crystal Structure of Mouse Protocadherin-15 EC9-10

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
B	0005509	molecular_function	calcium ion binding
B	0005886	cellular_component	plasma membrane
B	0007155	biological_process	cell adhesion
B	0007156	biological_process	homophilic cell-cell adhesion
B	0016020	cellular_component	membrane
B	0098609	biological_process	cell-cell adhesion
C	0005509	molecular_function	calcium ion binding
C	0005886	cellular_component	plasma membrane
C	0007155	biological_process	cell adhesion
C	0007156	biological_process	homophilic cell-cell adhesion
C	0016020	cellular_component	membrane
C	0098609	biological_process	cell-cell adhesion
D	0005509	molecular_function	calcium ion binding
D	0005886	cellular_component	plasma membrane
D	0007155	biological_process	cell adhesion
D	0007156	biological_process	homophilic cell-cell adhesion
D	0016020	cellular_component	membrane
D	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 2001

Chain	Residue
A	ASN899
A	TYR901
A	ASP931
A	ASP933
A	ALA939
A	ASP989

---

site_id	AC2
Number of Residues	5
Details	binding site for residue CA A 2002

Chain	Residue
A	GLU1116
A	ASP1118
A	GLU1026
A	GLU1077
A	ASP1115

---

site_id	AC3
Number of Residues	3
Details	binding site for residue CA A 2003

Chain	Residue
A	GLU1026
A	ASP1075
A	ASP1118

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA B 2001

Chain	Residue
B	ASN899
B	TYR901
B	ASP931
B	ASP933
B	ALA939
B	ASP989

---

site_id	AC5
Number of Residues	6
Details	binding site for residue CA B 2002

Chain	Residue
B	GLU1026
B	GLU1077
B	ASP1115
B	GLU1116
B	ASP1118
B	CA2003

---

site_id	AC6
Number of Residues	5
Details	binding site for residue CA B 2003

Chain	Residue
B	GLU1026
B	ASP1075
B	GLU1077
B	ASP1118
B	CA2002

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CA C 2001

Chain	Residue
C	ASN899
C	TYR901
C	ASP931
C	ASP933
C	ALA939
C	ASP989

---

site_id	AC8
Number of Residues	5
Details	binding site for residue CA C 2002

Chain	Residue
C	GLU1026
C	GLU1077
C	ASP1115
C	GLU1116
C	ASP1118

---

site_id	AC9
Number of Residues	4
Details	binding site for residue CA C 2003

Chain	Residue
C	GLU1026
C	ASP1075
C	GLU1077
C	ASP1118

---

site_id	AD1
Number of Residues	6
Details	binding site for residue CA D 2001

Chain	Residue
D	ASN899
D	TYR901
D	ASP931
D	ASP933
D	ALA939
D	ASP989

---

site_id	AD2
Number of Residues	5
Details	binding site for residue CA D 2002

Chain	Residue
D	GLU1026
D	GLU1077
D	ASP1115
D	GLU1116
D	ASP1118

---

site_id	AD3
Number of Residues	4
Details	binding site for residue CA D 2003

Chain	Residue
D	GLU1026
D	ASP1075
D	GLU1077
D	ASP1118

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE1111-PRO1121

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	432
Details	Domain: {"description":"Cadherin 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	214
Details	Domain: {"description":"Cadherin 10","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---