2p5i

X-ray diffraction
2.21Å resolution

Crystal structure of protein BH3822 from Bacillus halodurans, a member of the biotin/lipoate A/B protein ligase family

Released:
Entry authors: Sugadev R, Burley SK, Swaminathan S, New York SGX Research Center for Structural Genomics (NYSGXRC)

Function and Biology Details

Reaction catalysed:
[Glycine cleavage system H]-N(6)-octanoyl-L-lysine + a [lipoyl-carrier protein] = glycine cleavage system H + a [lipoyl-carrier protein]-N(6)-octanoyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-191770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Octanoyl-[GcvH]:protein N-octanoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 288 amino acids
Theoretical weight: 32.53 KDa
Source organism: Alkalihalobacillus halodurans C-125
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9K6A7 (Residues: 2-278; Coverage: 100%)
Gene names: BH3822, lipL
Sequence domains: Biotin/lipoate A/B protein ligase family
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P65
Unit cell:
a: 87.715Å b: 87.715Å c: 78.878Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.263
Expression system: Escherichia coli BL21(DE3)