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4NUP

Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005886cellular_componentplasma membrane
A0007155biological_processcell adhesion
A0007156biological_processhomophilic cell-cell adhesion
A0016020cellular_componentmembrane
A0098609biological_processcell-cell adhesion
B0005509molecular_functioncalcium ion binding
B0005886cellular_componentplasma membrane
B0007155biological_processcell adhesion
B0007156biological_processhomophilic cell-cell adhesion
B0016020cellular_componentmembrane
B0098609biological_processcell-cell adhesion
C0005509molecular_functioncalcium ion binding
C0005886cellular_componentplasma membrane
C0007155biological_processcell adhesion
C0007156biological_processhomophilic cell-cell adhesion
C0016020cellular_componentmembrane
C0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 301
ChainResidue
AGLU11
AASP67
AGLU69
AASP103
AHOH437

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 302
ChainResidue
AASP103
AASP136
AGLU11
AGLU69
AASP100
AMET101

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 303
ChainResidue
AASN102
AASN104
AASP134
AASP136
AASN142
AASP194

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 301
ChainResidue
BGLU11
BASP67
BGLU69
BASP103
BHOH408
BHOH415

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 302
ChainResidue
BGLU11
BGLU69
BASP100
BMET101
BASP103
BASP136

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 303
ChainResidue
BASN102
BASN104
BASP134
BASP136
BASN142
BASP194

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA C 301
ChainResidue
CGLU11
CASP67
CGLU69
CASP103

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 302
ChainResidue
CGLU11
CGLU69
CASP100
CMET101
CASP103
CASP136

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 303
ChainResidue
CASN102
CASN104
CASP134
CASP136
CASN142
CASP194

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 304
ChainResidue
BASP44
CGLU119
CASP215
CHOH459
CHOH506

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 Residues30
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"25253890","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21366346","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25253890","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21300292","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q2W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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