1vrg

X-ray diffraction
2.3Å resolution

Crystal structure of propionyl-CoA carboxylase, beta subunit (TM0716) from THERMOTOGA MARITIMA at 2.30 A resolution

Released:
Source organism: Thermotoga maritima MSB8
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reaction catalysed:
ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA
Biochemical function:
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Propionyl-CoA carboxylase, beta subunit Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 527 amino acids
Theoretical weight: 58.6 KDa
Source organism: Thermotoga maritima MSB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZH5 (Residues: 1-515; Coverage: 100%)
Gene name: TM_0716
Sequence domains: Carboxyl transferase domain
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 113.922Å b: 162.21Å c: 187.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.154 0.21
Expression system: Escherichia coli