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Structure of the alpha-tubulin acetyltransferase, alpha-TAT1

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

PDB: 4GS4
Type: protein
Length: 174 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
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alpha-tubulin N-acetyltransferase (EC 2.3.1.108)	protein	174	33% helix, 25% strand	Q5SQI0

Ligands and binding sites

ACO · Acetyl 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	249	0.66	0.83	28	ACO

Modifications

Observed in the structure: 3 modified (engineered).

Compared structures

4GS4 · Structure of the alpha-tubulin acetyltransferase, alpha-TAT1 · 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 0.97

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 4GS4 · PDBe 4GS4 · UniProt Q5SQI0

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