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5TFM

Crystal Structure of Human Cadherin-23 EC6-8

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
A0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 901
ChainResidue
AASN642
AASN644
AASP674
AASP676
ATYR681
AASP727

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 902
ChainResidue
AGLU641
AASP643
AASP676
AGLU549
AGLU607
AASP640

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 903
ChainResidue
AGLU549
AASP605
AGLU607
AASP643
AHOH1006

site_idAC4
Number of Residues5
Detailsbinding site for residue NA A 904
ChainResidue
AGLU659
AASP712
AGLU714
AASP750
AHOH1009

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 905
ChainResidue
AGLU659
AGLU714
AASP747
AILE748
AASP750
AASP783

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 906
ChainResidue
AASN749
AASN751
AASP781
AASP783
AASN787
AASP839

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeVfDeNDNpP
ChainResidueDetails
AILE636-PRO646
AILE743-PRO753

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues112
DetailsDomain: {"description":"Cadherin 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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