MolNFT v1 · #150608 · protein
Transcription factor dimerization activates the P300 acetyltransferase
6GYT · Histone acetyltransferase P300: “Transcription factor dimerization activates the P300 acetyltransferase”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.64). MolNFT v1 #150608 on GenesisL1: 3D structure, binding…
- PDB
- 6GYT
- Type
- protein
- Length
- 338 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase P300; Histone H4
- EC
- 2.3.1.48, 2.3.1.-
- UniProt
- Q09472
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 53% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase P300 (EC 2.3.1.48, 2.3.1.-) | protein | 161 | 55% helix, 4% strand | Q09472 |
| B | Histone acetyltransferase P300 (EC 2.3.1.48, 2.3.1.-) | protein | 168 | 54% helix, 4% strand | Q09472 |
| C | Histone H4 | protein | 9 | 0% helix, 0% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 284 | 0.64 | 0.81 | 39 | empty |
| 2 | 88 | 0.47 | 0.81 | 21 | empty |
Interfaces
2 interfaces between chains.
- A–B · 743 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 442 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
- 6GYT · Transcription factor dimerization activates the p300 acetyltransferase · the same entry in another collection · chain A against A, TM-score 1.00
- Q09472 · AlphaFold monomer V2.0 prediction for histone acetyltransferase P300 (Q09472) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q09472
- Elsewhere: RCSB PDB 6GYT · PDBe 6GYT · UniProt Q09472
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