MolNFT v1 · #104072 · protein
Crystal structure of P300 histone acetyltransferase domain in complex with acetyl-coenzyme a
4PZS · Histone acetyltransferase P300: “Crystal structure of P300 histone acetyltransferase domain in complex with acetyl-coenzyme a”. X-ray diffraction, 1 ligand (ACO), 3 pockets (best druggability 0.71). MolNFT v1 #104072 on GenesisL1…
- PDB
- 4PZS
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase P300
- EC
- 2.3.1.48
- UniProt
- Q09472
- Ligands
- ACO
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase P300 (EC 2.3.1.48) | protein | 334 | 43% helix, 20% strand | Q09472 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.71 | 0.82 | 45 | ACO |
| 2 | 226 | 0.59 | 0.80 | 33 | DMS |
| 3 | 69 | 0.32 | 0.75 | 15 | empty |
Compared structures
- 4PZS · Crystal structure of p300 histone acetyltransferase domain in complex with… · 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 0.99
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 4PZS · PDBe 4PZS · UniProt Q09472
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