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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 v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
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 · 1 distinct chain · 35% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-tubulin N-acetyltransferase 1 (EC 2.3.1.108)	protein	182	35% helix, 25% strand	Q5SQI0

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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	268	0.66	0.82	30	COA

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

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 4U9Z · PDBe 4U9Z · UniProt Q5SQI0

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