Research workbench
Crystal structure of alpha-tubulin acetyltransferase domain of human mec-17 in complex with acetoacetyl-CoA (P21212 form)
Analyse Crystal structure of alpha-tubulin acetyltransferase domain of human mec-17 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VWD
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- 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, CL
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-tubulin N-acetyltransferase (EC 2.3.1.108) | protein | 196 | 33% helix, 22% strand | Q5SQI0 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
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 | 268 | 0.64 | 0.81 | 30 | ACO |
| 2 | 92 | 0.38 | 0.75 | 13 | EDO |
Compared structures
- 3VWD · Crystal structure of alpha-tubulin acetyltransferase domain of human Mec-17 in complex… · 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 0.96
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 Q5SQI0
- Elsewhere: RCSB PDB 3VWD · PDBe 3VWD · UniProt Q5SQI0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.