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5IU9

Crystal Structure of Zebrafish Protocadherin-19 EC1-4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell-cell adhesion
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue CA A 1001
ChainResidue
AGLU10
AGLU11
AASP65
AASP67
AASP101

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 1002
ChainResidue
AASP101
AASP134
AGLU10
AASP67
AASP98
AVAL99

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 1003
ChainResidue
AASN100
AASN102
AASP132
AASP134
AASN138
AASP189

site_idAC4
Number of Residues4
Detailsbinding site for residue CA A 1004
ChainResidue
AGLU117
AASP174
AGLU176
AASP210

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 1005
ChainResidue
AGLU117
AGLU176
AASP207
ASER208
AASP210
AASP243

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 1006
ChainResidue
AASN209
AASN211
AASP241
AASP243
AASN247
AASP297

site_idAC7
Number of Residues5
Detailsbinding site for residue CA A 1007
ChainResidue
AGLU226
AASP282
AGLU284
AASP318
AASN319

site_idAC8
Number of Residues6
Detailsbinding site for residue CA A 1008
ChainResidue
AGLU226
AGLU284
AASP315
AILE316
AASP318
AASP354

site_idAC9
Number of Residues6
Detailsbinding site for residue CA A 1009
ChainResidue
AASN317
AASN319
AASP352
AASP354
AASN358
AASP404

site_idAD1
Number of Residues4
Detailsbinding site for residue NA A 1010
ChainResidue
AASP236
ALEU237
AASN238
ATHR272

site_idAD2
Number of Residues5
Detailsbinding site for residue CA B 1001
ChainResidue
BGLU10
BGLU11
BASP65
BASP67
BASP101

site_idAD3
Number of Residues6
Detailsbinding site for residue CA B 1002
ChainResidue
BGLU10
BASP67
BASP98
BVAL99
BASP101
BASP134

site_idAD4
Number of Residues6
Detailsbinding site for residue CA B 1003
ChainResidue
BASN100
BASN102
BASP132
BASP134
BASN138
BASP189

site_idAD5
Number of Residues4
Detailsbinding site for residue CA B 1004
ChainResidue
BGLU117
BASP174
BGLU176
BASP210

site_idAD6
Number of Residues6
Detailsbinding site for residue CA B 1005
ChainResidue
BGLU117
BGLU176
BASP207
BSER208
BASP210
BASP243

site_idAD7
Number of Residues6
Detailsbinding site for residue CA B 1006
ChainResidue
BASN209
BASN211
BASP241
BASP243
BASN247
BASP297

site_idAD8
Number of Residues5
Detailsbinding site for residue CA B 1007
ChainResidue
BGLU226
BASP282
BGLU284
BASP318
BASN319

site_idAD9
Number of Residues6
Detailsbinding site for residue CA B 1008
ChainResidue
BGLU226
BGLU284
BASP315
BILE316
BASP318
BASP354

site_idAE1
Number of Residues7
Detailsbinding site for residue CA B 1009
ChainResidue
BASN319
BALA320
BASP352
BASP354
BASN358
BASP404
BASN317

site_idAE2
Number of Residues4
Detailsbinding site for residue NA B 1010
ChainResidue
BASP236
BLEU237
BASN238
BTHR272

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeIiDvNDNaP
ChainResidueDetails
AILE94-PRO104
AILE203-PRO213
AVAL311-PRO321

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues216
DetailsDomain: {"description":"Cadherin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues214
DetailsDomain: {"description":"Cadherin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues46
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27787195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues24
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27787195","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34520737","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PGW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5IU9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34520737","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PGW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues10
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues99
DetailsDomain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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