X-ray diffraction
2.2Å resolution

Crystal structure of accD5 (Rv3280), an acyl-CoA carboxylase beta- subunit from Mycobacterium tuberculosis

Entry author: Holton SJ

Function and Biology Details

Reaction catalysed:
[Biotin carboxyl-carrier protein]-N(6)-carboxybiotinyl-L-lysine + acetyl-CoA = [biotin carboxyl-carrier protein]-N(6)-biotinyl-L-lysine + malonyl-CoA
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 548 amino acids
Theoretical weight: 59.36 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
  • Canonical: P9WQH7 (Residues: 1-548; Coverage: 100%)
Gene names: MTCY71.20, Rv3280, accD5, pccB
Sequence domains: Carboxyl transferase domain
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P41212
Unit cell:
a: 173.562Å b: 173.562Å c: 339.823Å
α: 90° β: 90° γ: 90°
R R work R free
0.178 0.176 0.211
Expression system: Escherichia coli