› 2fah

X-ray diffraction
2.09Å resolution

The structure of mitochondrial PEPCK, Complex with Mn and GDP

Released:
DOI: 10.2210/pdb2fah/pdb
PDB entry 2fah coloured by chain, front view.
PDB entry 2fah coloured by chain, side view.
PDB entry 2fah coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structural insights into the mechanism of PEPCK catalysis.
Holyoak T, Sullivan SM, Nowak T
Biochemistry 45 8254-63 (2006)
PMID: 16819824

Function and Biology Details

Reaction catalysed: 
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149338 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Phosphoenolpyruvate carboxykinase [GTP], mitochondrial Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 608 amino acids
Theoretical weight: 67.39 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P21642 (Residues: 34-128, 130-641; Coverage: 95%)
Gene name: PCK2
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: TQY, FRU
Ligand TQY 2 x TQY
Ligand FRU 2 x FRU
3 bound ligands:
Ligand GDP 4 x GDP
Ligand MLA 5 x MLA
Ligand MN 8 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P1
Unit cell:
a: 74.595Å b: 90.852Å c: 103.339Å
α: 64.23° β: 73.74° γ: 71.18°
R-values:
R R work R free
0.189 0.187 0.234

Quick links

Citations

6 review citations

Physiological functions of mineral micronutrients (Cu, Zn, Mn, Fe, Ni, Mo, B, Cl).
Hänsch et al. (2009)
5 more

1 mention without citation

Computational evaluation of natural compounds as potential inhibitors of human PEPCK-M: an alternative for lung cancer therapy.
Baptista et al. (2019)