Research workbench
Tubulin acetyltransferase
Analyse Tubulin acetyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4H6Z
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-tubulin N-acetyltransferase
- EC
- 2.3.1.108
- UniProt
- Q6PH17
- Ligands
- ACO, PO4
- Pockets
- 4 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tubulin N-acetyltransferase (EC 2.3.1.108) | protein | 147 | 27% helix, 39% strand | Q6PH17 |
| B | Alpha-tubulin N-acetyltransferase (EC 2.3.1.108) | protein | 145 | 23% helix, 37% strand | Q6PH17 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.77 | 0.98 | 20 | empty |
| 2 | 270 | 0.57 | 0.77 | 27 | ACO |
| 3 | 231 | 0.55 | 0.77 | 27 | ACO |
| 4 | 53 | 0.28 | 0.75 | 15 | PO4 |
Interfaces
1 interface between chains.
- A–B · 1466 Ų buried · 27 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
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 Q6PH17
- Elsewhere: RCSB PDB 4H6Z · PDBe 4H6Z · UniProt Q6PH17
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