MolNFT v1 · #48339 · protein
Myst histone acetyltransferase 1
2PQ8 · Probable histone acetyltransferase MYST1: “Myst histone acetyltransferase 1”. X-ray diffraction, 3 ligands (COA, ZN, UNX), 2 pockets (best druggability 0.67). MolNFT v1 #48339 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 2PQ8
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable histone acetyltransferase MYST1
- EC
- 2.3.1.48
- UniProt
- Q9H7Z6
- Ligands
- COA, ZN, UNX
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable histone acetyltransferase MYST1 (EC 2.3.1.48) | protein | 260 | 37% helix, 24% strand | Q9H7Z6 |
Ligands and binding sites
- COA · Coenzyme A · ligand · chains A
- ZN · Zinc ion · metal · chains A
- UNX · Unknown atom or ion · ion · 13 copies · chains A
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 | 296 | 0.67 | 0.82 | 33 | COA, UNX |
| 2 | 52 | 0.31 | 0.76 | 13 | empty |
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 Q9H7Z6
- Elsewhere: RCSB PDB 2PQ8 · PDBe 2PQ8 · UniProt Q9H7Z6
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