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4EHP

Crystal Structure of human vinculin head domain (residues 1-252) in complex with alpha-catenin (residues 277-382)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003779molecular_functionactin binding
A0005198molecular_functionstructural molecule activity
A0007155biological_processcell adhesion
A0015629cellular_componentactin cytoskeleton
A0051015molecular_functionactin filament binding
B0007155biological_processcell adhesion
B0045296molecular_functioncadherin binding
B0051015molecular_functionactin filament binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACT A 301
ChainResidue
ATHR6
AILE9
AASP127
AHOH447
BARG330

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 302
ChainResidue
AASP39
ALEU250
ATHR251
ASER252

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 303
ChainResidue
AILE245
AGLN249
AHOH454

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 304
ChainResidue
ASER207
ALYS228
AASN229

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 305
ChainResidue
AVAL32
ALYS35
ATYR100
ASER101
AARG105
BTYR351

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 306
ChainResidue
ATHR197
AGLU200

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 307
ChainResidue
ATHR65
APHE126
ALYS133
BARG329

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACT A 308
ChainResidue
ALYS87
AASP110

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ACT A 309
ChainResidue
APRO2
AGLN90
ATYR107
ATHR183
AGLN185
AGLU186

Functional Information from PROSITE/UniProt
site_idPS00663
Number of Residues21
DetailsVINCULIN_1 Vinculin family talin-binding region signature. KnLgpgMtkMakmideRQQEL
ChainResidueDetails
ALYS162-LEU182

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER295
BSER297

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS173

218500

PDB entries from 2024-04-17

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