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6BXU

Crystal Structure of Mouse Protocadherin-15 EC5-7 I582T

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 Residues6
Detailsbinding site for residue CA A 901
ChainResidue
AGLN590
ASER591
AASP621
AGLU623
AASP625
AASP671

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 902
ChainResidue
AASP691
AASN692
ACA903
AGLU606
AASP656
AGLU658

site_idAC3
Number of Residues7
Detailsbinding site for residue CA A 903
ChainResidue
AGLU606
AGLU658
AASP688
AVAL689
AASP691
AASP724
ACA902

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 904
ChainResidue
AASN690
AASN692
AASP722
AASP724
AASN728
AASP772

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 905
ChainResidue
AASN482
AASN484
AASP514
AASP516
AASN520
AASP566

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 901
ChainResidue
BGLN590
BSER591
BASP621
BGLU623
BASP625
BASP671

site_idAC7
Number of Residues6
Detailsbinding site for residue CA B 902
ChainResidue
BASN690
BASN692
BASP722
BASP724
BASN728
BASP772

site_idAC8
Number of Residues4
Detailsbinding site for residue CA B 903
ChainResidue
BGLU606
BASP656
BGLU658
BASP691

site_idAC9
Number of Residues7
Detailsbinding site for residue CA B 904
ChainResidue
BGLU606
BARG657
BGLU658
BASP688
BVAL689
BASP691
BASP724

site_idAD1
Number of Residues6
Detailsbinding site for residue CA B 905
ChainResidue
BASN482
BASN484
BASP514
BASP516
BASN520
BASP566

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IvVtDvNDNaP
ChainResidueDetails
AILE684-PRO694

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN538
AASN641
AASN703
AASN747
BASN538
BASN641
BASN703
BASN747

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PDB entries from 2024-06-12

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