1lw1

X-ray diffraction
2.3Å resolution

Crystal Structure Of Mycobacterium Tuberculosis Alkylperoxidase Ahpd H137F mutant

Released:

Function and Biology Details

Reaction catalysed:
A [lipoyl-carrier protein]-N(6)-((R)-dihydrolipoyl)-L-lysine + ROOH = a [lipoyl-carrier protein]-N(6)-((R)-lipoyl)-L-lysine + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alkyl hydroperoxide reductase AhpD Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 177 amino acids
Theoretical weight: 18.81 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P9WQB5 (Residues: 1-177; Coverage: 100%)
Gene names: MTCY428.17c, Rv2429, ahpD
Sequence domains: Carboxymuconolactone decarboxylase family
Structure domains: AhpD-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2
Unit cell:
a: 96.603Å b: 62.184Å c: 89.481Å
α: 90° β: 121.81° γ: 90°
R-values:
R R work R free
0.196 0.184 0.286
Expression system: Escherichia coli BL21