MolNFT v1 · #19723 · protein
Histone acetyltransferase HPA2 from saccharomyces cerevisiae
1QSO · HPA2 histone acetyltransferase: “Histone acetyltransferase HPA2 from saccharomyces cerevisiae”. X-ray diffraction, 5 pockets (best druggability 0.79). MolNFT v1 #19723 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QSO
- Type
- protein
- Length
- 596 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HPA2 histone acetyltransferase
- EC
- 2.3.1.48
- UniProt
- Q06592
- Pockets
- 5 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | HPA2 histone acetyltransferase (EC 2.3.1.48) | protein | 149 | 34% helix, 30% strand | Q06592 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 799 | 0.79 | 0.82 | 98 | empty |
| 2 | 1050 | 0.79 | 0.80 | 110 | empty |
| 3 | 251 | 0.71 | 0.86 | 36 | empty |
| 4 | 84 | 0.37 | 0.76 | 14 | empty |
| 5 | 71 | 0.32 | 0.75 | 13 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2987 Ų buried · 59 hydrogen bonds · protein-protein
- A–B · 2929 Ų buried · 53 hydrogen bonds · protein-protein
- B–D · 358 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 330 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 85 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1QSO · Histone Acetyltransferase HPA2 from Saccharomyces Cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- Q06592 · AlphaFold monomer V2.0 prediction for histone acetyltransferase HPA2 (Q06592) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q06592
- Elsewhere: RCSB PDB 1QSO · PDBe 1QSO · UniProt Q06592
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