MolNFT v1 · #47515 · protein
Human histone acetyltransferase 1 (HAT1)
2P0W · Histone acetyltransferase type B catalytic subunit: “Human histone acetyltransferase 1 (HAT1)”. X-ray diffraction, 3 ligands (ACM, ACO, CL), 7 pockets (best druggability 0.59). MolNFT v1 #47515 on GenesisL1: 3D structure, binding…
- PDB
- 2P0W
- Type
- protein
- Length
- 665 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase type B catalytic subunit; Histone peptide H4
- EC
- 2.3.1.48
- UniProt
- O14929
- Ligands
- ACM, ACO, CL
- Pockets
- 7 · best druggability 0.59
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) | protein | 319 | 35% helix, 29% strand | O14929 |
| B | Histone acetyltransferase type B catalytic subunit (EC 2.3.1.48) | protein | 317 | 39% helix, 29% strand | O14929 |
| P | Histone peptide H4 | protein | 15 | 0% helix, 0% strand | — |
| Q | Histone peptide H4 | protein | 14 | 0% helix, 0% strand | — |
Ligands and binding sites
- ACM · Acetamide · ligand · 4 copies · chains A, B
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, P, B, Q
- CL · Chloride ion · ion · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 217 | 0.59 | 0.80 | 30 | ACO |
| 2 | 219 | 0.58 | 0.80 | 28 | ACO |
| 3 | 276 | 0.56 | 0.76 | 25 | empty |
| 4 | 103 | 0.41 | 0.76 | 20 | ACT |
| 5 | 86 | 0.38 | 0.76 | 21 | empty |
Interfaces
3 interfaces between chains.
- B–Q · 807 Ų buried · 26 hydrogen bonds · protein-protein
- A–P · 790 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 487 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
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 O14929
- Elsewhere: RCSB PDB 2P0W · PDBe 2P0W · UniProt O14929
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