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2O72

Crystal Structure Analysis of human E-cadherin (1-213)

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 401
ChainResidue
AASN102
AASN104
AASP134
AASP136
AASN143
AASP195

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AGLN101
AASP103
AASP136
AGLU11
AGLU69
AASP100

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AGLU11
AASP67
AGLU69
AASP103
AHOH428
AHOH479

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AGLN110
AGLU119
AASP180
ACA405
AHOH624
AHOH639

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
AGLU119
AARG181
AGLU182
AASP213
ACA404
AHOH546
AHOH624

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP103
AASP134

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by S.pyogenes SpeB => ECO:0000269|PubMed:23532847
ChainResidueDetails
ATHR210

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000250|UniProtKB:P09803
ChainResidueDetails
ASER126

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000250|UniProtKB:P09803
ChainResidueDetails
ATHR131
ATHR204

226707

PDB entries from 2024-10-30

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