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1I7W

BETA-CATENIN/PHOSPHORYLATED E-CADHERIN COMPLEX

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0045296molecular_functioncadherin binding
B0005509molecular_functioncalcium ion binding
B0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
B0098609biological_processcell-cell adhesion
C0007155biological_processcell adhesion
C0045296molecular_functioncadherin binding
D0005509molecular_functioncalcium ion binding
D0007156biological_processhomophilic cell adhesion via plasma membrane adhesion molecules
D0098609biological_processcell-cell adhesion
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 1
ChainResidue
AHIS176
ACYS213
AHOH905

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 2
ChainResidue
CHIS176
CARG212
CCYS213

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 701
ChainResidue
CARG449
CARG453
AGLY277
AILE314
AHOH747

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 702
ChainResidue
CLYS335
CARG376
CHOH974
DSER690
DHOH733

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 703
ChainResidue
ALYS312
AHOH973

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 704
ChainResidue
AARG376
BSER690

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 705
ChainResidue
APRO321
AGLN322

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 706
ChainResidue
CGLY319
CPRO321
CGLN322

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 707
ChainResidue
ATYR331
ATHR332
ATYR333

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 708
ChainResidue
AHOH923
CGLY268
CALA269
CLYS270
CMET271

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues300
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
BARG578-ASP728
DARG578-ASP728

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Cleavage; by caspase-3 => ECO:0000250
ChainResidueDetails
BASP596
DASP596

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000250|UniProtKB:P12830
ChainResidueDetails
BTYR599
BTYR600
BTYR601
DTYR599
DTYR600
DTYR601

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P12830
ChainResidueDetails
BSER616
BSER639
DSER616
DSER639

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:19759396
ChainResidueDetails
BSEP684
BSEP686
BSEP692
DSEP684
DSEP686
DSEP692

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P35222
ChainResidueDetails
ATHR556
CTHR556

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:20705246
ChainResidueDetails
ACYS619
CCYS619

222036

PDB entries from 2024-07-03

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