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5KJ4

Crystal Structure of Mouse Protocadherin-15 EC9-10

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
A0098609biological_processcell-cell adhesion
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0016020cellular_componentmembrane
B0098609biological_processcell-cell adhesion
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
C0016020cellular_componentmembrane
C0098609biological_processcell-cell adhesion
D0005509molecular_functioncalcium ion binding
D0005886cellular_componentplasma membrane
D0007155biological_processcell adhesion
D0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
D0016020cellular_componentmembrane
D0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 2001
ChainResidue
AASN899
ATYR901
AASP931
AASP933
AALA939
AASP989

site_idAC2
Number of Residues5
Detailsbinding site for residue CA A 2002
ChainResidue
AGLU1116
AASP1118
AGLU1026
AGLU1077
AASP1115

site_idAC3
Number of Residues3
Detailsbinding site for residue CA A 2003
ChainResidue
AGLU1026
AASP1075
AASP1118

site_idAC4
Number of Residues6
Detailsbinding site for residue CA B 2001
ChainResidue
BASN899
BTYR901
BASP931
BASP933
BALA939
BASP989

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 2002
ChainResidue
BGLU1026
BGLU1077
BASP1115
BGLU1116
BASP1118
BCA2003

site_idAC6
Number of Residues5
Detailsbinding site for residue CA B 2003
ChainResidue
BGLU1026
BASP1075
BGLU1077
BASP1118
BCA2002

site_idAC7
Number of Residues6
Detailsbinding site for residue CA C 2001
ChainResidue
CASN899
CTYR901
CASP931
CASP933
CALA939
CASP989

site_idAC8
Number of Residues5
Detailsbinding site for residue CA C 2002
ChainResidue
CGLU1026
CGLU1077
CASP1115
CGLU1116
CASP1118

site_idAC9
Number of Residues4
Detailsbinding site for residue CA C 2003
ChainResidue
CGLU1026
CASP1075
CGLU1077
CASP1118

site_idAD1
Number of Residues6
Detailsbinding site for residue CA D 2001
ChainResidue
DASN899
DTYR901
DASP931
DASP933
DALA939
DASP989

site_idAD2
Number of Residues5
Detailsbinding site for residue CA D 2002
ChainResidue
DGLU1026
DGLU1077
DASP1115
DGLU1116
DASP1118

site_idAD3
Number of Residues4
Detailsbinding site for residue CA D 2003
ChainResidue
DGLU1026
DASP1075
DGLU1077
DASP1118

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IeIqDeNDHpP
ChainResidueDetails
AILE1111-PRO1121

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN1043
AASN1063
BASN1043
BASN1063
CASN1043
CASN1063
DASN1043
DASN1063

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PDB entries from 2024-10-30

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