› 2fm4

Solution NMR

NMR structure of the phosphoryl carrier domain of pyruvate phosphate dikinase

Released:
DOI: 10.2210/pdb2fm4/pdb
PDB entry 2fm4 coloured by chain, ensemble of 11 models, front view.
PDB entry 2fm4 coloured by chain, ensemble of 11 models, side view.
PDB entry 2fm4 coloured by chain, ensemble of 11 models, top view.
Source organism: [Clostridium] symbiosum
Primary publication:
Examination of the structure, stability, and catalytic potential in the engineered phosphoryl carrier domain of pyruvate phosphate dikinase.
Lin Y, Lusin JD, Ye D, Dunaway-Mariano D, Ames JB
Biochemistry 45 1702-11 (2006)
PMID: 16460017

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate + phosphate = AMP + phosphoenolpyruvate + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate, phosphate dikinase Chain: A
Molecule details ›
Chain: A
Length: 128 amino acids
Theoretical weight: 13.11 KDa
Source organism: [Clostridium] symbiosum
Expression system: Escherichia coli
UniProt:
  • Canonical: P22983 (Residues: 384-511; Coverage: 15%)
Gene name: ppdK
Sequence domains: PEP-utilising enzyme, mobile domain
Structure domains: Phosphohistidine domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The ATP-grasp enzymes.
Fawaz et al. (2011)
3 other articles

1 mention without citation

Structural intermediates and directionality of the swiveling motion of Pyruvate Phosphate Dikinase.
Minges et al. (2017)