Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5CO1

Crystal Structure of Zebrafish Protocadherin-19 EC3-4

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
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 adhesion via plasma membrane adhesion molecules
B	0016020	cellular_component	membrane
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 adhesion via plasma membrane adhesion molecules
C	0016020	cellular_component	membrane
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 adhesion via plasma membrane adhesion molecules
D	0016020	cellular_component	membrane

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA A 1001

Chain	Residue
A	GLU226
A	ASP282
A	GLU284
A	ASP318
A	HOH1104
A	HOH1108

site_id	AC2
Number of Residues	6
Details	binding site for residue CA A 1002

Chain	Residue
A	ILE316
A	ASP318
A	ASP354
A	GLU226
A	GLU284
A	ASP315

site_id	AC3
Number of Residues	6
Details	binding site for residue CA A 1003

Chain	Residue
A	ASN317
A	ASN319
A	ASP352
A	ASP354
A	ASN358
A	ASP404

site_id	AC4
Number of Residues	5
Details	binding site for residue CA A 1004

Chain	Residue
A	ASP236
A	LEU237
A	THR272
A	HOH1101
A	HOH1109

site_id	AC5
Number of Residues	6
Details	binding site for residue CA B 501

Chain	Residue
B	GLU226
B	ASP282
B	GLU284
B	ASP318
B	HOH610
B	HOH613

site_id	AC6
Number of Residues	6
Details	binding site for residue CA B 502

Chain	Residue
B	GLU226
B	GLU284
B	ASP315
B	ILE316
B	ASP318
B	ASP354

site_id	AC7
Number of Residues	6
Details	binding site for residue CA B 503

Chain	Residue
B	ASN317
B	ASN319
B	ASP352
B	ASP354
B	ASN358
B	ASP404

site_id	AC8
Number of Residues	6
Details	binding site for residue CA B 504

Chain	Residue
B	ASP236
B	LEU237
B	THR272
B	HOH603
B	HOH608
B	HOH614

site_id	AC9
Number of Residues	6
Details	binding site for residue CA C 501

Chain	Residue
C	GLU226
C	ASP282
C	GLU284
C	ASP318
C	HOH606
C	HOH611

site_id	AD1
Number of Residues	6
Details	binding site for residue CA C 502

Chain	Residue
C	GLU226
C	GLU284
C	ASP315
C	ILE316
C	ASP318
C	ASP354

site_id	AD2
Number of Residues	6
Details	binding site for residue CA C 503

Chain	Residue
C	ASN317
C	ASN319
C	ASP352
C	ASP354
C	ASN358
C	ASP404

site_id	AD3
Number of Residues	6
Details	binding site for residue CA C 504

Chain	Residue
C	ASP236
C	LEU237
C	THR272
C	HOH608
C	HOH609
C	HOH613

site_id	AD4
Number of Residues	5
Details	binding site for residue CA D 501

Chain	Residue
D	GLU226
D	ASP282
D	GLU284
D	ASP318
D	HOH603

site_id	AD5
Number of Residues	6
Details	binding site for residue CA D 502

Chain	Residue
D	GLU226
D	GLU284
D	ASP315
D	ILE316
D	ASP318
D	ASP354

site_id	AD6
Number of Residues	6
Details	binding site for residue CA D 503

Chain	Residue
D	ASN317
D	ASN319
D	ASP352
D	ASP354
D	ASN358
D	ASP404

site_id	AD7
Number of Residues	5
Details	binding site for residue CA D 504

Chain	Residue
D	ASP236
D	LEU237
D	THR272
D	HOH605
D	HOH609

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL311-PRO321

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	BINDING: BINDING => ECO:0000269\|PubMed:27787195, ECO:0000269\|PubMed:34520737, ECO:0000312\|PDB:6PGW, ECO:0007744\|PDB:5IU9

Chain	Residue	Details
A	GLU226
A	ASP354
A	ASN358
A	ASP404
B	GLU226
B	ASP282
B	GLU284
B	ASP315
B	ILE316
B	ASN317
B	ASP318
A	ASP282
B	ASN319
B	ASP352
B	ASP354
B	ASN358
B	ASP404
C	GLU226
C	ASP282
C	GLU284
C	ASP315
C	ILE316
A	GLU284
C	ASN317
C	ASP318
C	ASN319
C	ASP352
C	ASP354
C	ASN358
C	ASP404
D	GLU226
D	ASP282
D	GLU284
A	ASP315
D	ASP315
D	ILE316
D	ASN317
D	ASP318
D	ASN319
D	ASP352
D	ASP354
D	ASN358
D	ASP404
A	ILE316
A	ASN317
A	ASP318
A	ASN319
A	ASP352

site_id	SWS_FT_FI2
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269\|PubMed:27787195, ECO:0007744\|PDB:5IU9

Chain	Residue	Details
A	ASP241
D	ASP241
D	ASP243
D	ASN247
A	ASP243
A	ASN247
B	ASP241
B	ASP243
B	ASN247
C	ASP241
C	ASP243
C	ASN247

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269\|PubMed:34520737, ECO:0007744\|PDB:6PGW

Chain	Residue	Details
A	GLU337
C	ASP389
C	GLU391
C	ASP422
D	GLU337
D	ASP389
D	GLU391
D	ASP422
A	ASP389
A	GLU391
A	ASP422
B	GLU337
B	ASP389
B	GLU391
B	ASP422
C	GLU337

site_id	SWS_FT_FI4
Number of Residues	16
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255\|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN238
C	ASN260
C	ASN353
C	ASN397
D	ASN238
D	ASN260
D	ASN353
D	ASN397
A	ASN260
A	ASN353
A	ASN397
B	ASN238
B	ASN260
B	ASN353
B	ASN397
C	ASN238

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)