MolNFT v1 · #86406 · protein
Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant
4B5P · Alpha-tubulin N-acetyltransferase: “Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant”. X-ray diffraction, 2 ligands (ACO, NA), 2 pockets (best druggability 0.75). MolNFT v1 #86406 on…
- PDB
- 4B5P
- Type
- protein
- Length
- 368 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
- Q5SQI0
- Ligands
- ACO, NA
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tubulin N-acetyltransferase (EC 2.3.1.108) | protein | 184 | 33% helix, 23% strand | Q5SQI0 |
| B | Alpha-tubulin N-acetyltransferase (EC 2.3.1.108) | protein | 184 | 33% helix, 25% strand | Q5SQI0 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 499 | 0.75 | 0.83 | 47 | NA, ACO |
| 2 | 457 | 0.75 | 0.84 | 48 | ACO |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4B5P · Crystal structure of human alpha tubulin acetyltransferase catalytic domain Q58A variant · the same entry in another collection · chain A against A, TM-score 1.00
- Q5SQI0 · AlphaFold monomer V2.0 prediction for alpha-tubulin N-acetyltransferase 1 (Q5SQI0) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q5SQI0
- Elsewhere: RCSB PDB 4B5P · PDBe 4B5P · UniProt Q5SQI0
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