UniProt Q12432
Chromatin modification-related protein EAF3 (Q12432)
Chromatin modification-related protein EAF3 (UniProt Q12432): 20 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 70 pockets. Binding sites, druggability and experiment against prediction (TM-score) in…
- UniProt
- Q12432
- Protein
- Chromatin modification-related protein EAF3
- Experimental structures
- 20
- Predicted models
- 1
- Ligands
- 1
- Pockets
- 70 · 10 records with a druggable one
Structures
21 records of Q12432 in the MolNFT archive: 20 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 2K3X | Solution structure of EAF3 chromo barrel domain | solution nmr | A | — | — |
| 2K3X | Solution structure of EAF3 chromo barrel domain | solution nmr | A | — | — |
| 2K3Y | Solution structure of EAF3 chromo barrel domain bound to histone h3 with a dimethyllysine analog… | solution nmr | A | — | — |
| 2K3Y | Solution structure of EAF3 chromo barrel domain bound to histone H3 with a dimethyllysine analog… | solution nmr | A | — | — |
| 3E9F | Crystal structure short-form (residue1-113) of Eaf3 chromo domain | x-ray diffraction | A | — | — |
| 3E9F | Crystal structure short-form (RESIDUE1-113) of EAF3 chromo domain | x-ray diffraction | A | — | — |
| 3E9G | Crystal structure long-form (residue1-124) of Eaf3 chromo domain | x-ray diffraction | A, B | — | — |
| 3E9G | Crystal structure long-form (RESIDUE1-124) of EAF3 chromo domain | x-ray diffraction | A, B | — | — |
| 6K5W | Solution structure of the chromodomain of yeast Eaf3 | solution nmr | A | — | — |
| 6K5W | Solution structure of the chromodomain of yeast EAF3 | solution nmr | A | — | — |
| 7YI2 | Cryo-EM structure of Rpd3S in loose-state Rpd3S-NCP complex | electron microscopy | C | ZN | 6 (best 0.82) |
| 7YI4 | Cryo-EM structure of Rpd3S complex bound to H3K36me3 nucleosome in close state | electron microscopy | C, E | ZN | 6 (best 0.78) |
| 7YI5 | Cryo-EM structure of Rpd3S complex bound to H3K36me3 nucleosome in loose state | electron microscopy | C, E | ZN | 6 (best 0.78) |
| 8KC7 | Rpd3S histone deacetylase complex | electron microscopy | D, F | — | 9 (best 0.79) |
| 8KD3 | Rpd3S in complex with nucleosome with H3K36MLA modification, H3K9Q mutation and 187bp DNA | electron microscopy | D, F | — | 9 (best 0.83) |
| 8KD5 | Rpd3S in complex with nucleosome with H3K36MLA modification and 187bp DNA, class2 | electron microscopy | D, F | — | 9 (best 0.81) |
| 8TOF | Rpd3S bound to an H3K36Cme3 modified nucleosome | electron microscopy | D, E | ZN | 8 (best 0.81) |
| 8W9C | Cryo-EM structure of the Rpd3S complex from budding yeast | electron microscopy | C, D | ZN | 8 (best 0.73) |
| 8W9D | Cryo-EM structure of the Rpd3S-nucleosome complex from budding yeast in State 1 | electron microscopy | C, D, G | ZN | 4 (best 0.75) |
| 8W9F | Cryo-EM structure of the Rpd3S-nucleosome complex from budding yeast in State 3 | electron microscopy | C, D, G | ZN | 5 (best 0.76) |
| Q12432 | AlphaFold monomer V2.0 prediction for chromatin modification-related protein EAF3 (Q12432) | predicted | A | — | — |
Ligands
- ZN · Zinc ion · in 7 records
Experiment against prediction
- 8W9D chain G against the predicted model Q12432: TM-score 1.00, RMSD 0.00 Å
- 8W9F chain G against the predicted model Q12432: TM-score 1.00, RMSD 0.00 Å
- 8W9F chain D against the predicted model Q12432: TM-score 0.99, RMSD 0.61 Å
- 3E9G chain A against the predicted model Q12432: TM-score 0.97, RMSD 0.68 Å
- 3E9G chain A against the predicted model Q12432: TM-score 0.97, RMSD 0.68 Å
- 3E9G chain B against the predicted model Q12432: TM-score 0.97, RMSD 0.74 Å
- 3E9G chain B against the predicted model Q12432: TM-score 0.97, RMSD 0.74 Å
- 3E9F chain A against the predicted model Q12432: TM-score 0.97, RMSD 0.99 Å
- 3E9F chain A against the predicted model Q12432: TM-score 0.97, RMSD 0.99 Å
- 8W9C chain D against the predicted model Q12432: TM-score 0.97, RMSD 0.94 Å
Elsewhere
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.