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2A62

Crystal structure of mouse cadherin-8 EC1-3

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 323
ChainResidue
AASN100
AASN102
AASP132
AASP134
ASER141
AASP187

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 324
ChainResidue
AILE99
AASP101
AASN102
AASP134
ACA325
AGLU11
AGLU66
AASP98

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 325
ChainResidue
AGLU11
AGLU12
AASP64
AGLU66
AASP101
ACA324

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 326
ChainResidue
AASN209
AASN211
AASP241
AASP243
AASN247
AASN298

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 327
ChainResidue
AGLU117
AASP207
AVAL208
AASP210
AASP243
ACA328

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 328
ChainResidue
AGLU117
AARG173
AGLU174
AASP207
AASP210
AASP243
ACA327

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. IkVqDiNDNaP
ChainResidueDetails
AILE94-PRO104
AVAL203-PRO213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN127

225946

PDB entries from 2024-10-09

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