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1NCH

STRUCTURAL BASIS OF CELL-CELL ADHESION BY CADHERINS

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 Residues3
DetailsBINDING SITE FOR RESIDUE YB A 500
ChainResidue
AGLU11
AASP67
AGLU69

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE YB B 600
ChainResidue
BGLU11
BGLU69
BASP100
BHOH676

site_idYB
Number of Residues1
Details
ChainResidue
AYB500

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ
ChainResidueDetails
AGLU11
BGLU69
BASP100
BMET101
BASN102
BASN104
AASP67
AGLU69
AASP100
AMET101
AASN102
AASN104
BGLU11
BASP67

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21366346, ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ
ChainResidueDetails
AASP103
BASP103

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN31
BASN31

219140

PDB entries from 2024-05-01

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