4op0

X-ray diffraction
1.7Å resolution

Crystal structure of biotin protein ligase (RV3279C) of Mycobacterium tuberculosis, complexed with biotinyl-5'-AMP

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Possible bifunctional protein BirA: biotin operon repressor + biotin--[acetyl-CoA-carboxylase] synthetase (Biotin--protein ligase) Chains: A, B
Molecule details ›
Chains: A, B
Length: 268 amino acids
Theoretical weight: 28.25 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: I6YFP0 (Residues: 3-266; Coverage: 99%)
Gene names: Rv3279c, birA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 41.737Å b: 75.406Å c: 77.599Å
α: 90° β: 97.92° γ: 90°
R-values:
R R work R free
0.194 0.192 0.242
Expression system: Escherichia coli BL21(DE3)