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Structure of the alpha-tubulin acetyltransferase alpha-TAT1/Mec-17 in complex with CoA

Analyse Structure of the alpha-tubulin acetyltransferase alpha-TAT1/Mec-17 in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4U9Z
Type
protein
Length
182 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.802
Source
Homo sapiens
Molecule
Alpha-tubulin N-acetyltransferase 1
EC
2.3.1.108
UniProt
Q5SQI0
Ligands
COA
Pockets
1 · best druggability 0.66

Structure

x-ray diffraction · resolution 1.802 · 1 distinct chain · 35% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-tubulin N-acetyltransferase 1 (EC 2.3.1.108)protein18235% helix, 25% strandQ5SQI0

Ligands and binding sites

  • COA · Coenzyme A · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12680.660.8230COA

Compared structures

  • 4U9Z · Structure of the alpha-tubulin acetyltransferase alpha-TAT1/MEC-17 in complex with CoA · 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

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