PDBe 2c81

X-ray diffraction
1.7Å resolution

Crystal structures of the PLP- and PMP-bound forms of BtrR, a dual functional aminotransferase involved in butirosin biosynthesis.

Released:

Function and Biology Details

Reactions catalysed:
L-glutamine + 3-amino-2,3-dideoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxystreptamine. 
L-glutamine + 2-deoxy-scyllo-inosose = 2-oxoglutaramate + 2-deoxy-scyllo- inosamine. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-glutamine:2-deoxy-scyllo-inosose aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 418 amino acids
Theoretical weight: 47.09 KDa
Source organism: Bacillus circulans
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8G8Y2 (Residues: 1-418; Coverage: 100%)
Gene names: btrR, btrS
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 73.75Å b: 73.75Å c: 162.36Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 0.209
Expression system: Escherichia coli BL21