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6DV1

Crystal structure of the alpha-E-catenin actin-binding domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0007155biological_processcell adhesion
A0045296molecular_functioncadherin binding
A0051015molecular_functionactin filament binding
B0007155biological_processcell adhesion
B0045296molecular_functioncadherin binding
B0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues2
Detailsbinding site for residue BR A 1001
ChainResidue
ALYS683
ALYS704

site_idAC2
Number of Residues1
Detailsbinding site for residue BR A 1002
ChainResidue
AHIS766

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 1003
ChainResidue
ASER668
AARG670
ALYS737
AHOH1120

site_idAC4
Number of Residues3
Detailsbinding site for residue BR B 1001
ChainResidue
BHOH1134
BSER668
BARG670

site_idAC5
Number of Residues3
Detailsbinding site for residue BR B 1002
ChainResidue
BGLN692
BMET724
BTHR727

site_idAC6
Number of Residues1
Detailsbinding site for residue BR B 1003
ChainResidue
AGLN678

site_idAC7
Number of Residues5
Detailsbinding site for residue SO4 B 1004
ChainResidue
ALEU785
AHIS788
BTYR779
BARG782
BGLN831

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER652
ASER655
BSER652
BSER655

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ATHR658
BTHR658

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P35221
ChainResidueDetails
ASER851
BSER851

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P35221
ChainResidueDetails
ALYS797
BLYS797

221716

PDB entries from 2024-06-26

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