MolNFT v1 · #175314 · protein
The crystal structure of human MYST1 from biortus.
7CMR · Histone acetyltransferase KAT8: “The crystal structure of human MYST1 from biortus.”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.68). MolNFT v1 #175314 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 7CMR
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT8
- EC
- 2.3.1.48
- UniProt
- Q9H7Z6
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT8 (EC 2.3.1.48) | protein | 263 | 35% helix, 25% strand | Q9H7Z6 |
Ligands and binding sites
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 | 206 | 0.68 | 0.85 | 37 | GOL |
| 2 | 68 | 0.38 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 1 modified (acetylation).
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 7CMR · PDBe 7CMR · UniProt Q9H7Z6
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