Research workbench
Crystal structure of moz double phd finger histone H3K14AC complex
Analyse Crystal structure of moz double phd finger histone H3K14AC complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LLB
- Type
- protein
- Length
- 276 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histone acetyltransferase KAT6A; Histone H3.1
- EC
- 2.3.1.48
- UniProt
- Q92794, P68431
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 18% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Histone acetyltransferase KAT6A (EC 2.3.1.48) | protein | 123 | 14% helix, 8% strand | Q92794 |
| C, D | Histone H3.1 | protein | 15 | 53% helix, 7% strand | P68431 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.53 | 0.86 | 16 | empty |
| 2 | 61 | 0.53 | 0.87 | 19 | empty |
| 3 | 248 | 0.47 | 0.73 | 28 | empty |
Interfaces
3 interfaces between chains.
- B–D · 881 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 879 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 207 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (acetylation).
Compared structures
- 4LLB · Crystal Structure of MOZ double PHD finger histone H3K14ac complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q92794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase KAT6A (Q92794) · a predicted model of the same protein · chain A against A, TM-score 0.96
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
- Every structure of UniProt P68431
- Elsewhere: RCSB PDB 4LLB · PDBe 4LLB · UniProt Q92794 · UniProt P68431
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