› 4rcg

X-ray diffraction
2.6Å resolution

Crystal Structure Analysis of MTB PEPCK without Mn+2

Released:
DOI: 10.2210/pdb4rcg/pdb
PDB entry 4rcg coloured by chain, front view.
PDB entry 4rcg coloured by chain, side view.
PDB entry 4rcg coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis.
Machová I, Snášel J, Dostál J, Brynda J, Fanfrlík J, Singh M, Tarábek J, Vaněk O, Bednárová L, Pichová I
PLoS One 10 e0120682 (2015)
PMID: 25798914

Function and Biology Details

Reaction catalysed: 
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161626 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase [GTP] Chain: A
Molecule details ›
Chain: A
Length: 626 amino acids
Theoretical weight: 69.51 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WIH3 (Residues: 1-606; Coverage: 100%)
Gene names: MTCY08D5.06, Rv0211, pck1, pckA, pckG
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GDP 1 x GDP
Ligand MG 1 x MG
Ligand PEG 3 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: C2221
Unit cell:
a: 104.412Å b: 124.277Å c: 121.635Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.271
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

The PEP-pyruvate-oxaloacetate node: variation at the heart of metabolism.
Koendjbiharie et al. (2021)
1 more

2 mentions without citation

Structural and functional studies of phosphoenolpyruvate carboxykinase from Mycobacterium tuberculosis.
Machová et al. (2015)
1 more