UniProt P15108
ATP-dependent molecular chaperone HSC82 (P15108)
ATP-dependent molecular chaperone HSC82 (UniProt P15108): 9 experimental structures on GenesisL1, 5 ligands bound, 58 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P15108
- Protein
- ATP-dependent molecular chaperone HSC82
- Experimental structures
- 9
- Predicted models
- 0
- Ligands
- 5
- Pockets
- 58 · 3 records with a druggable one
Structures
9 records of P15108 in the MolNFT archive: 9 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 6XLC | Full-length HSC82 bound to amppnp | electron microscopy | A, B | ANP, MG | 18 (best 0.82) |
| 6XLD | Full-length Hsc82 in complex with Aha1 CTD in the presence of AMPPNP | electron microscopy | A, B | ANP, MG | 20 (best 0.81) |
| 6XLD | Full-length HSC82 in complex with AHA1 ctd in the presence of amppnp | electron microscopy | A, B | ANP, MG | — |
| 6XLE | Full-length HSC82 in complex with two AHA1 ctd in the presence of AMP- pnp | electron microscopy | A, B | ANP, MG, K | — |
| 6XLF | Full-length HSC82 in complex with AHA1 in the presence of AMP-pnp | electron microscopy | A, B | ANP, MG, K | — |
| 6XLG | Full-length HSC82 in complex with two AHA1 ctd in the presence of atpgammas | electron microscopy | A, B | AGS, MG, K | — |
| 6XLH | Asymmetric hydrolysis state of Hsc82 in complex with Aha1 bound with ADP and ATPgammaS | electron microscopy | A, B | AGS, MG, K, ADP | 20 (best 0.84) |
| 6XLH | Asymmetric hydrolysis state of HSC82 in complex with AHA1 bound with ADP and atpgammas | electron microscopy | A, B | AGS, MG, K, ADP | — |
| P15108 | AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSC82 (P15108) | — | — | — |
Ligands
Elsewhere
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