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6CGU

mouse cadherin-6 EC1-2 adhesive fragment

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 301
ChainResidue
AGLU11
AGLU12
AASP64
AGLU66
AASP101
AHOH563

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 302
ChainResidue
AILE99
AASP101
AASP134
AGLU11
AGLU66
AASP98

site_idAC3
Number of Residues6
Detailsbinding site for residue CA A 303
ChainResidue
AASN100
AASN102
AASP132
AASP134
ASER141
AASP187

site_idAC4
Number of Residues6
Detailsbinding site for residue CA B 301
ChainResidue
BASN100
BASN102
BASP132
BASP134
BSER141
BASP187

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 302
ChainResidue
BGLU11
BGLU66
BASP98
BILE99
BASP101
BASP134

site_idAC6
Number of Residues6
Detailsbinding site for residue CA B 303
ChainResidue
BGLU11
BGLU12
BASP64
BGLU66
BASP101
BHOH621

site_idAC7
Number of Residues4
Detailsbinding site for residue CA C 301
ChainResidue
CASN170
CARG173
CASN175
CHOH606

site_idAC8
Number of Residues6
Detailsbinding site for residue CA C 302
ChainResidue
CGLU11
CGLU66
CASP98
CILE99
CASP101
CASP134

site_idAC9
Number of Residues6
Detailsbinding site for residue CA C 303
ChainResidue
CGLU11
CGLU12
CASP64
CGLU66
CASP101
CHOH617

site_idAD1
Number of Residues6
Detailsbinding site for residue CA C 304
ChainResidue
CASN100
CASN102
CASP132
CASP134
CSER141
CASP187

site_idAD2
Number of Residues6
Detailsbinding site for residue CA D 301
ChainResidue
DGLU11
DGLU66
DASP98
DILE99
DASP101
DASP134

site_idAD3
Number of Residues6
Detailsbinding site for residue CA D 302
ChainResidue
DASN100
DASN102
DASP132
DASP134
DSER141
DASP187

site_idAD4
Number of Residues6
Detailsbinding site for residue CA D 303
ChainResidue
DGLU11
DGLU12
DASP64
DGLU66
DASP101
DHOH546

site_idAD5
Number of Residues3
Detailsbinding site for residue CA D 304
ChainResidue
DGLU117
DASP172
DASN175

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IkIhDiNDNeP
ChainResidueDetails
AILE94-PRO104

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN202
BASN202
CASN202
DASN202

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PDB entries from 2024-07-24

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