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Crystal structure of moz double phd finger
Analyse Crystal structure of moz double phd finger in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LJN
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6A
- EC
- 2.3.1.48
- UniProt
- Q92794
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 120 | 13% helix, 10% strand | Q92794 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.62 | 0.92 | 18 | empty |
| 2 | 53 | 0.34 | 0.78 | 15 | empty |
| 3 | 52 | 0.28 | 0.74 | 16 | 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 Q92794
- Elsewhere: RCSB PDB 4LJN · PDBe 4LJN · UniProt Q92794
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