2c7t

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE PLP-BOUND FORM OF BTRR, A DUAL FUNCTIONAL AMINOTRANSFERASE INVOLVED IN BUTIROSIN BIOSYNTHESIS.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-184463 (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: Niallia circulans
Expression system: Escherichia coli BL21(DE3)
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


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P3221
Unit cell:
a: 73.74Å b: 73.74Å c: 162.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.206
Expression system: Escherichia coli BL21(DE3)