2zxv

X-ray diffraction
2.3Å resolution

Crystal structure of putative acetyltransferase from T. thermophilus HB8

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 194 amino acids
Theoretical weight: 22.29 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SHD1 (Residues: 1-194; Coverage: 100%)
Gene name: TTHA1799
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: I4
Unit cell:
a: 127.8Å b: 127.8Å c: 122.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.228 0.266
Expression system: Escherichia coli