4q0g

X-ray diffraction
2.31Å resolution

Crystal structure of beta subunit of acyl-CoA carboxylase AccD1 from Mycobacterium tuberculosis

Released:
Source organism: Mycobacterium tuberculosis
Entry authors: Bie HY, Yin J, James MNG, TB Structural Genomics Consortium (TBSGC)

Function and Biology Details

Reaction catalysed:
ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl-CoA

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable acetyl-/propionyl-CoA carboxylase (Beta subunit) AccD1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 529 amino acids
Theoretical weight: 56.84 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: I6YDK7 (Residues: 1-529; Coverage: 100%)
Gene names: Rv2502c, accD1
Sequence domains: Carboxyl transferase domain
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2221
Unit cell:
a: 142.571Å b: 221.253Å c: 167.835Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.213
Expression system: Escherichia coli