5VH2

Crystal Structure of Mouse Cadherin-23 EC12-13 with Engineered Mutation S1339D

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
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	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	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	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	5
Details	binding site for residue CA A 1401

Chain	Residue
A	GLU1181
A	ASP1212
A	ASP1214
A	GLY1218
A	ASP1264

---

site_id	AC2
Number of Residues	7
Details	binding site for residue CA A 1402

Chain	Residue
A	ASP1285
A	ASP1318
A	CA1403
A	GLU1197
A	GLU1251
A	ASN1282
A	GLU1283

---

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 1403

Chain	Residue
A	GLU1197
A	ASP1249
A	GLU1251
A	ASP1285
A	GLU1286
A	CA1402

---

site_id	AC4
Number of Residues	5
Details	binding site for residue NA A 1404

Chain	Residue
A	GLU1286
A	ALA1287
A	ASP1316
A	ASP1318
A	ASP1370

---

site_id	AC5
Number of Residues	5
Details	binding site for residue CA B 1401

Chain	Residue
B	GLU1181
B	ASP1212
B	ASP1214
B	GLY1218
B	ASP1264

---

site_id	AC6
Number of Residues	5
Details	binding site for residue CA B 1402

Chain	Residue
B	GLU1197
B	ASP1249
B	GLU1251
B	ASP1285
B	GLU1286

---

site_id	AC7
Number of Residues	6
Details	binding site for residue CA B 1403

Chain	Residue
B	GLU1197
B	GLU1251
B	ASN1282
B	GLU1283
B	ASP1285
B	ASP1318

---

site_id	AC8
Number of Residues	5
Details	binding site for residue NA B 1404

Chain	Residue
B	GLU1286
B	ALA1287
B	ASP1316
B	ASP1318
B	ASP1370

---

site_id	AC9
Number of Residues	5
Details	binding site for residue CA C 1401

Chain	Residue
C	GLU1197
C	ASP1249
C	GLU1251
C	ASP1285
C	GLU1286

---

site_id	AD1
Number of Residues	6
Details	binding site for residue CA C 1402

Chain	Residue
C	GLU1197
C	GLU1251
C	ASN1282
C	GLU1283
C	ASP1285
C	ASP1318

---

site_id	AD2
Number of Residues	5
Details	binding site for residue NA C 1403

Chain	Residue
C	GLU1286
C	ALA1287
C	ASP1316
C	ASP1318
C	ASP1370

---

site_id	AD3
Number of Residues	6
Details	binding site for residue CA D 1401

Chain	Residue
D	GLU1197
D	GLU1251
D	ASN1282
D	GLU1283
D	ASP1285
D	ASP1318

---

site_id	AD4
Number of Residues	5
Details	binding site for residue CA D 1402

Chain	Residue
D	GLU1197
D	ASP1249
D	GLU1251
D	ASP1285
D	GLU1286

---

site_id	AD5
Number of Residues	5
Details	binding site for residue NA D 1403

Chain	Residue
D	GLU1286
D	ALA1287
D	ASP1316
D	ASP1318
D	ASP1370

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	206
Details	Domain: {"description":"Cadherin 12","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---