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UniProt O05209

VCP-like ATPase (O05209)

VCP-like ATPase (UniProt O05209): 13 experimental structures on GenesisL1, 2 ligands bound, 60 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
O05209
Protein
VCP-like ATPase
Experimental structures
13
Predicted models
0
Ligands
2
Pockets
60 · 3 records with a druggable one

Structures

13 records of O05209 in the MolNFT archive: 13 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1CZ4NMR structure of vat-N: the N-terminal domain of vat (vcp-like ATPase of thermoplasma)solution nmrA——
1CZ4NMR structure of vat-N: the N-terminal domain of vat (vcp-like ATPase of thermoplasma)solution nmrA——
1CZ5NMR structure of vat-N: the N-terminal domain of vat (vcp-like ATPase of thermoplasma)solution nmrA——
1CZ5NMR structure of vat-N: the N-terminal domain of vat (vcp-like ATPase of thermoplasma)solution nmrA——
5G4FStructure of the ADP-bound VAT complexelectron microscopyA, B, C, D, E, P—20 (best 0.85)
5G4FStructure of the ADP-bound vat complexelectron microscopyA, B, C, D, E, P——
5G4GStructure of the atpgs-bound vat complexelectron microscopyA, B, C, D, E, F——
5VC7VCP like ATPase from T. acidophilum (VAT) - conformation 1electron microscopyA, C, D, E, F, GATP20 (best 0.82)
5VC7Vcp like ATPase from T. acidophilum (vat) - conformation 1electron microscopyA, C, D, E, F, GATP—
5VCAVCP like ATPase from T. acidophilum (VAT)-Substrate bound conformationelectron microscopyP, M, N, O, Q, R—20 (best 0.85)
5VCAVcp like ATPase from T. acidophilum (vat)-substrate bound conformationelectron microscopyP, M, N, O, Q, R——
7DBODpbb domain of vcp-like ATPase from thermoplasma acidophilumx-ray diffractionA, BSO4—
O05209AlphaFold monomer V2.0 prediction for vcp-like ATPase (O05209)———

Ligands

  • ATP · Adenosine-5'-triphosphate · in 2 records
  • SO4 · Sulfate ion · in 1 record

Elsewhere

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