6jhu

X-ray diffraction
1.97Å resolution

Crystal Structure Of Biotin Protein Ligase From Leishmania Major in complex with Biotinyl-5-AMP

Released:
Source organism: Leishmania major

Function and Biology Details

Reaction catalysed:
ATP + biotin + [biotin carboxyl-carrier protein]-L-lysine = AMP + diphosphate + [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BPL/LPL catalytic domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 30.56 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4Q6F6 (Residues: 1-263; Coverage: 100%)
Gene name: LMJF_31_1070
Sequence domains: Biotin/lipoate A/B protein ligase family

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 116.848Å b: 46.621Å c: 54.573Å
α: 90° β: 104.569° γ: 90°
R-values:
R R work R free
0.218 0.217 0.248
Expression system: Escherichia coli BL21(DE3)