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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 adhesion via plasma membrane adhesion molecules
A0016020cellular_componentmembrane
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
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 Residues46
DetailsBINDING: BINDING => ECO:0000269|PubMed:27787195, ECO:0007744|PDB:5IU9
ChainResidueDetails
AGLU10
AGLU117
AASP132
AASP134
AASN138
AGLU176
AASP189
AASP207
ASER208
AASN209
AASP210
AGLU11
AASN211
AASP241
AASP243
AASN247
BGLU10
BGLU11
BASP65
BASP67
BASP98
BVAL99
AASP65
BASN100
BASP101
BASN102
BGLU117
BASP132
BASP134
BASN138
BGLU176
BASP189
BASP207
AASP67
BSER208
BASN209
BASP210
BASN211
BASP241
BASP243
BASN247
AASP98
AVAL99
AASN100
AASP101
AASN102

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:27787195, ECO:0000269|PubMed:34520737, ECO:0000312|PDB:6PGW, ECO:0007744|PDB:5IU9
ChainResidueDetails
AGLU226
AASP354
AASN358
AASP404
BGLU226
BASP282
BGLU284
BASP315
BILE316
BASN317
BASP318
AASP282
BASN319
BASP352
BASP354
BASN358
BASP404
AGLU284
AASP315
AILE316
AASN317
AASP318
AASN319
AASP352

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:34520737, ECO:0007744|PDB:6PGW
ChainResidueDetails
AGLU337
AASP389
AGLU391
AASP422
BGLU337
BASP389
BGLU391
BASP422

site_idSWS_FT_FI4
Number of Residues10
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN20
BASN397
AASN238
AASN260
AASN353
AASN397
BASN20
BASN238
BASN260
BASN353

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PDB entries from 2024-07-17

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