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1FF5

STRUCTURE OF E-CADHERIN DOUBLE DOMAIN

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
BASN102
BASN104
BASP134
BASP136
BASN143
BASP195

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
BGLN101
BASP103
BASP136
BGLU11
BGLU69
BASP100

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
BGLU11
BASN12
BASP67
BGLU69
BASP103
BHOH1060
BHOH1115

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1004
ChainResidue
AASN102
AASN104
AASP134
AASP136
AASN143
AASP195

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1005
ChainResidue
AGLU11
AGLU69
AASP100
AGLN101
AASP103
AASP136

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1006
ChainResidue
AGLU11
AASN12
AASP67
AGLU69
AASP103

Functional Information from PROSITE/UniProt
site_idPS00232
Number of Residues11
DetailsCADHERIN_1 Cadherin domain signature. ItVtDqNDNrP
ChainResidueDetails
AILE96-PRO106

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AASP103
AASP134
BASP103
BASP134

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:28973932
ChainResidueDetails
ASER126
ASER131
BSER126
BSER131

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:28973932
ChainResidueDetails
ATHR204
BTHR204

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PDB entries from 2024-10-30

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