GL1X · GenesisL1 explorer

UniProt P0A6H5

Protein (heat shock locus U) (P0A6H5)

Protein (heat shock locus U) (UniProt P0A6H5): 19 experimental structures and 1 predicted model on GenesisL1, 5 ligands bound, 43 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P0A6H5
Protein
Protein (heat shock locus U)
Experimental structures
19
Predicted models
1
Ligands
5
Pockets
43 · 3 records with a druggable one

Structures

20 records of P0A6H5 in the MolNFT archive: 19 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1DO0Orthorhombic crystal form of heat shock locus U (hslu) from escherichia COLIx-ray diffractionA, B, C, D, E, FATP, MG, SO420 (best 0.87)
1DO0Orthorhombic crystal form of heat shock locus U (hslu) from escherichia COLIx-ray diffractionA, B, C, D, E, F——
1DO2Trigonal crystal form of heat shock locus U (hslu) from escherichia COLIx-ray diffractionA, B, C, DANP15 (best 0.86)
1DO2Trigonal crystal form of heat shock locus U (hslu) from escherichia COLIx-ray diffractionA, B, C, D——
1G4ACrystal structures of the hslvu peptidase-ATPase complex reveal an ATP-dependent proteolysis…x-ray diffractionE, F——
1G4ACrystal structures of the hslvu peptidase-ATPase complex reveal an ATP-dependent proteolysis…x-ray diffractionE, F——
1G4BCrystal structures of the hslvu peptidase-ATPase complex reveal an ATP-dependent proteolysis…x-ray diffractionE, F, K, L——
1G4BCrystal structures of the hslvu peptidase-ATPase complex reveal an ATP-dependent proteolysis…x-ray diffractionE, F, K, L——
1HQYNucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslUx-ray diffractionE, F——
1HQYNucleotide-dependent conformational changes in a protease-associated ATPase hslux-ray diffractionE, F——
1HT1Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslUx-ray diffractionE, F, G, I——
1HT1Nucleotide-dependent conformational changes in a protease-associated ATPase hslux-ray diffractionE, F, G, I——
1HT2Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslUx-ray diffractionE, F, G, H——
1HT2Nucleotide-dependent conformational changes in a protease-associated ATPase hslux-ray diffractionE, F, G, H——
1YYFCorrection of X-ray Intensities from an HslV-HslU co-crystal containing lattice translocation…x-ray diffractionA, B——
1YYFCorrection of X-ray intensities from an hslv-hslu co- crystal containing lattice translocation…x-ray diffractionA, B——
5TXVHslU P21 cell with 4 hexamersx-ray diffractionA, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, XADP—
5TXVHslu P21 cell with 4 hexamersx-ray diffractionA, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, XADP—
6PXIThe crystal structure of a singly capped HslUV complex with an axial pore plug and a HslU E257Q…x-ray diffractionE, FADP8 (best 0.87)
P0A6H5AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit hslu (P0A6H5)predictedA——

Ligands

  • ADP · Adenosine-5'-diphosphate · in 3 records
  • ANP · Phosphoaminophosphonic acid-adenylate ester · in 1 record
  • ATP · Adenosine-5'-triphosphate · in 1 record
  • MG · Magnesium ion · in 1 record
  • SO4 · Sulfate ion · in 1 record

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.