Research workbench
Molecular basis for the autoregulation of the protein acetyl transferase RTT109
Analyse Molecular basis for the autoregulation of the protein acetyl transferase RTT109 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CZ7
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of TY1 transposition protein 109
- UniProt
- Q07794
- Ligands
- ACO
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of TY1 transposition protein 109 | protein | 364 | 31% helix, 26% strand | Q07794 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.71 | 0.84 | 41 | ACO |
| 2 | 188 | 0.66 | 0.85 | 29 | empty |
| 3 | 120 | 0.44 | 0.77 | 18 | empty |
| 4 | 51 | 0.30 | 0.76 | 14 | empty |
| 5 | 52 | 0.29 | 0.75 | 10 | empty |
Modifications
Observed in the structure: 6 modified (engineered, acetylation).
Compared structures
- 3CZ7 · Molecular Basis for the Autoregulation of the Protein Acetyl Transferase Rtt109 · the same entry in another collection · chain A against A, TM-score 1.00
- Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · a predicted model of the same protein · chain A against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q07794
- Elsewhere: RCSB PDB 3CZ7 · PDBe 3CZ7 · UniProt Q07794
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