4u9y

X-ray diffraction
2.2Å resolution

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

Released:
Source organism: Homo sapiens
Entry authors: Yuzawa S, Sumimoto H

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + [alpha-tubulin]-L-lysine = CoA + [alpha-tubulin]-N(6)-acetyl-L-lysine
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tubulin N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 201 amino acids
Theoretical weight: 22.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SQI0 (Residues: 1-194; Coverage: 46%)
Gene names: ATAT1, C6orf134, MEC17, Nbla00487
Sequence domains: GNAT acetyltransferase, Mec-17
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21212
Unit cell:
a: 42.849Å b: 121.938Å c: 37.397Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.23
Expression system: Escherichia coli BL21(DE3)