› 2qf7

X-ray diffraction
2Å resolution

Crystal structure of a complete multifunctional pyruvate carboxylase from Rhizobium etli

Released:
DOI: 10.2210/pdb2qf7/pdb
PDB entry 2qf7 coloured by chain, front view.
PDB entry 2qf7 coloured by chain, side view.
PDB entry 2qf7 coloured by chain, top view.
Source organism: Rhizobium etli CFN 42
Primary publication:
Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme.
St Maurice M, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I
Science 317 1076-9 (2007)
PMID: 17717183

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:

Ligands and Environments

7 bound ligands:
Ligand MG 6 x MG
Ligand ZN 2 x ZN
Ligand CL 4 x CL
Ligand COA 1 x COA
Ligand AGS 2 x AGS
Ligand FMT 2 x FMT
Ligand GOL 1 x GOL
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: C2
Unit cell:
a: 234.729Å b: 93.258Å c: 137.222Å
α: 90° β: 107.33° γ: 90°
R-values:
R R work R free
0.18 0.178 0.223
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Structure, mechanism and regulation of pyruvate carboxylase.
Jitrapakdee et al. (2008)
9 more

14 mentions without citation

Stable isotope-resolved metabolomics and applications for drug development.
Fan et al. (2012)
13 more