PDBe 4b5o

X-ray diffraction
1.05Å resolution

Crystal structure of human alpha tubulin acetyltransferase catalytic domain

Released:
Source organism: Homo sapiens
Primary publication:
Atomic resolution structure of human α-tubulin acetyltransferase bound to acetyl-CoA.
Proc. Natl. Acad. Sci. U.S.A. 109 19649-54 (2012)
PMID: 23071318

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:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-tubulin N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 200 amino acids
Theoretical weight: 22.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5SQI0 (Residues: 1-196; Coverage: 47%)
Gene names: ATAT1, C6orf134, MEC17, Nbla00487
Sequence domains: GNAT acetyltransferase, Mec-17
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand ACO 1 x ACO
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 42.198Å b: 121.958Å c: 37.277Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.131 0.157
Expression system: Escherichia coli BL21(DE3)