› 1m44

X-ray diffraction
1.6Å resolution

Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis-APO Structure

Released:
DOI: 10.2210/pdb1m44/pdb
PDB entry 1m44 coloured by chain, front view.
PDB entry 1m44 coloured by chain, side view.
PDB entry 1m44 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Aminoglycoside 2'-N-acetyltransferase from Mycobacterium tuberculosis in complex with coenzyme A and aminoglycoside substrates.
Vetting MW, Hegde SS, Javid-Majd F, Blanchard JS, Roderick SL
Nat Struct Biol 9 653-8 (2002)
PMID: 12161746

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-552499 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoglycoside 2'-N-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 181 amino acids
Theoretical weight: 20.06 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQG9 (Residues: 1-181; Coverage: 100%)
Gene names: MTCY06A4.06c, Rv0262c, aac
Sequence domains: Acetyltransferase (GNAT) domain
Structure domains: Aminopeptidase

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 42Å b: 68.5Å c: 120.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.201
Expression system: Escherichia coli

Quick links

Citations

17 review citations

Structure and functions of the GNAT superfamily of acetyltransferases.
Vetting et al. (2005)
16 more

10 mentions without citation

Aminoglycoside modifying enzymes.
Ramirez et al. (2010)
9 more