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

6PIM

Crystal Structure of Human Protocadherin-1 EC3-4

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 501
ChainResidue
AGLU234
AGLU291
AASP322
AMET323
AASP325
AASP366

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 502
ChainResidue
AASP366
AASN370
AASP423
AASN324
AASN326
AASP364

site_idAC3
Number of Residues4
Detailsbinding site for residue CA A 503
ChainResidue
AGLU234
AASP289
AGLU291
AASP325

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 504
ChainResidue
AASN217
AASN219
AASP249
AASP251
AASN255
AASP304

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. VtVkDmNDNaP
ChainResidueDetails
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

224004

PDB entries from 2024-08-21

PDB statisticsPDBj update infoContact PDBjnumon