› 3sma

X-ray diffraction
2Å resolution

A new N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF

Released:
DOI: 10.2210/pdb3sma/pdb
Model geometry
Fit model/data
PDB entry 3sma coloured by chain, front view.
PDB entry 3sma coloured by chain, side view.
PDB entry 3sma coloured by chain, top view.
Source organism: Streptomyces rubellomurinus
Primary publication:
New N-acetyltransferase fold in the structure and mechanism of the phosphonate biosynthetic enzyme FrbF.
Bae B, Cobb RE, DeSieno MA, Zhao H, Nair SK
J Biol Chem 286 36132-36141 (2011)
PMID: 21865168

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CMP-5'-(N-hydroxy-3-aminopropyl)phosphonate acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 286 amino acids
Theoretical weight: 31.59 KDa
Source organism: Streptomyces rubellomurinus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0ZQ43 (Residues: 1-286; Coverage: 100%)
Gene names: VM95_23220, frbF
Sequence domains: Aminoglycoside 3-N-acetyltransferase

Ligands and Environments

1 bound ligand:
Ligand ACO 4 x ACO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P2
Unit cell:
a: 128.832Å b: 35.692Å c: 136.087Å
α: 90° β: 117.6° γ: 90°
R-values:
R R work R free
0.195 0.193 0.246
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Phosphonate biosynthesis and catabolism: a treasure trove of unusual enzymology.
Peck et al. (2013)
2 other articles

3 mentions without citation

A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.
Kumar et al. (2018)
2 more