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UniProt P12003

Vinculin (P12003)

Vinculin (UniProt P12003): 31 experimental structures on GenesisL1, 3 ligands bound, 16 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P12003
Protein
Vinculin
Experimental structures
31
Predicted models
0
Ligands
3
Pockets
16 · 1 record with a druggable one

Structures

31 records of P12003 in the MolNFT archive: 31 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1QKRCrystal structure of the vinculin tail and a pathway for activationx-ray diffractionA, B——
1QKRCrystal structure of the vinculin tail and a pathway for activationx-ray diffractionA, B——
1ST6Crystal structure of a cytoskeletal proteinx-ray diffractionA——
1ST6Crystal structure of a cytoskeletal proteinx-ray diffractionA——
1T01Vinculin complexed with the VBS1 helix from talinx-ray diffractionA——
1T01Vinculin complexed with the VBS1 helix from talinx-ray diffractionA——
1U6HVinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)x-ray diffractionA——
1U6HVinculin head (0-258) in complex with the talin vinculin binding site 2 (849-879)x-ray diffractionA——
1XWJVinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)x-ray diffractionA——
1XWJVinculin head (1-258) in complex with the talin vinculin binding site 3 (1945-1969)x-ray diffractionA——
1ZVZVinculin Head (0-258) in Complex with the Talin Rod Residue 820-844x-ray diffractionA——
1ZVZVinculin head (0-258) in complex with the talin rod residue 820-844x-ray diffractionA——
1ZW2Vinculin Head (0-258) in Complex with the Talin Rod residues 2345-2369x-ray diffractionA——
1ZW2Vinculin head (0-258) in complex with the talin rod residues 2345-2369x-ray diffractionA——
1ZW3Vinculin Head (0-258) in Complex with the Talin Rod residues 1630-1652x-ray diffractionA——
1ZW3Vinculin head (0-258) in complex with the talin rod residues 1630-1652x-ray diffractionA——
2GDCStructure of Vinculin VD1 / IpaA560-633 complexx-ray diffractionA——
2GDCStructure of vinculin VD1 / IPAA560-633 complexx-ray diffractionA——
3JBIMDFF model of the vinculin tail domain bound to F-actinelectron microscopyV——
3JBIMdff model of the vinculin tail domain bound to F-actinelectron microscopyV——
3ZDLVinculin head (1-258) in complex with a RIAM fragmentx-ray diffractionA——
3ZDLVinculin head (1-258) in complex with a riam fragmentx-ray diffractionA——
4E17Alpha-E-catenin is an autoinhibited molecule that co-activates vinculinx-ray diffractionA——
4E17Alpha-E-catenin is an autoinhibited molecule that co-activates vinculinx-ray diffractionA——
4E18Alpha-E-catenin is an autoinhibited molecule that co-activates vinculinx-ray diffractionA——
4E18Alpha-E-catenin is an autoinhibited molecule that co-activates vinculinx-ray diffractionA——
6FQ4Structure of Chlamydial virulence factor TarP and vinculin head domainx-ray diffractionA——
6FQ4Structure of chlamydial virulence factor tarp and vinculin head domainx-ray diffractionA——
6NR7Rerefinement of chicken vinculinx-ray diffractionASO4, KYG, PO416 (best 0.83)
6NR7Rerefinement of chicken vinculinx-ray diffractionASO4, KYG, PO4—
P12003AlphaFold monomer V2.0 prediction for vinculin (P12003)———

Ligands

  • KYG · (1R,2R,3S,4R,5R,6S)-4-{[(S)-[(2S)-2,3-dihydroxypropoxy](hydroxy)phosphoryl]oxy}-3,5,6-trihydroxycyclohexane-1,2-diyl bis[dihydrogen (phosphate)] · in 2 records
  • PO4 · Phosphate ion · in 2 records
  • SO4 · Sulfate ion · in 2 records

Elsewhere

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