› 6at2

X-ray diffraction
1.44Å resolution

E. coli phosphoenolpyruvate carboxykinase G209N mutant bound to thiosulfate

Released:
DOI: 10.2210/pdb6at2/pdb
PDB entry 6at2 coloured by chain, front view.
PDB entry 6at2 coloured by chain, side view.
PDB entry 6at2 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase.
Tang HYH, Shin DS, Hura GL, Yang Y, Hu X, Lightstone FC, McGee MD, Padgett HS, Yannone SM, Tainer JA
Biochemistry 57 6688-6700 (2018)
PMID: 30376300

Function and Biology Details

Reaction catalysed: 
ATP + oxaloacetate = ADP + 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-149561 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase (ATP) Chain: A
Molecule details ›
Chain: A
Length: 546 amino acids
Theoretical weight: 60.6 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P22259 (Residues: 1-540; Coverage: 100%)
Gene names: JW3366, b3403, pck, pckA
Sequence domains: Phosphoenolpyruvate carboxykinase
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ATP 1 x ATP
Ligand MN 1 x MN
Ligand MG 1 x MG
Ligand TRS 1 x TRS
Ligand THJ 1 x THJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 12.3.1
Spacegroup: C2
Unit cell:
a: 125.171Å b: 94.36Å c: 46.559Å
α: 90° β: 96.4° γ: 90°
R-values:
R R work R free
0.172 0.171 0.191
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Millisecond mix-and-quench crystallography (MMQX) enables time-resolved studies of PEPCK with remote data collection.
Clinger et al. (2021)

1 mention without citation

Structural Control of Nonnative Ligand Binding in Engineered Mutants of Phosphoenolpyruvate Carboxykinase.
Tang et al. (2018)