Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6BX7

Crystal Structure of Human Protocadherin-1 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
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EPE A 501
ChainResidue
AGLU155
ATRP186
ATYR189
AASP190

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 502
ChainResidue
AGLU9
AGLU10
AASP59
AGLU61
AASP106

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 503
ChainResidue
AGLU9
AGLU61
AASP103
AILE104
AASP106
AASP139

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 504
ChainResidue
AASN105
AASN107
AASP137
AASP139
AASN143
AASP197

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 505
ChainResidue
AGLU122
AASP182
AGLU184
AASP218
AHOH601
AHOH611

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 506
ChainResidue
AGLU122
AGLU184
AASP215
ATHR216
AASP218
AASP251

site_idAC7
Number of Residues6
Detailsbinding site for residue CA A 507
ChainResidue
AASN217
AASN219
AASP249
AASP251
AASN255
AASP304

site_idAC8
Number of Residues6
Detailsbinding site for residue CA A 508
ChainResidue
AGLU234
AASP289
AGLU291
AASP325
AASN326
AHOH603

site_idAC9
Number of Residues6
Detailsbinding site for residue CA A 509
ChainResidue
AGLU234
AGLU291
AASP322
AMET323
AASP325
AASP366

site_idAD1
Number of Residues6
Detailsbinding site for residue CA A 510
ChainResidue
AASN324
AASN326
AASP364
AASP366
AASN370
AASP423

site_idAD2
Number of Residues4
Detailsbinding site for residue CA A 511
ChainResidue
AGLU349
AASP408
AASP441
AVAL442

site_idAD3
Number of Residues5
Detailsbinding site for residue CA A 512
ChainResidue
AASP187
ASER188
AGLU369
ASER424
AASN426

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeVqDiNDNtP
ChainResidueDetails
AILE99-PRO109
AVAL211-PRO221
AVAL318-PRO328

site_idPS00830
Number of Residues17
DetailsGREAB_2 Prokaryotic transcription elongation factors signature 2. SenSPIGhSVIqvkaND
ChainResidueDetails
ASER233-ASP249

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN248

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN346

224931

PDB entries from 2024-09-11

PDB statisticsPDBj update infoContact PDBjnumon