› 1pkn

X-ray diffraction
2.9Å resolution

STRUCTURE OF RABBIT MUSCLE PYRUVATE KINASE COMPLEXED WITH MN2+, K+, AND PYRUVATE

Released:
DOI: 10.2210/pdb1pkn/pdb
PDB entry 1pkn coloured by chain, front view.
PDB entry 1pkn coloured by chain, side view.
PDB entry 1pkn coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structure of rabbit muscle pyruvate kinase complexed with Mn2+, K+, and pyruvate.
Larsen TM, Laughlin LT, Holden HM, Rayment I, Reed GH
Biochemistry 33 6301-9 (1994)
PMID: 8193145

Function and Biology Details

Reactions catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 57.8 KDa
Source organism: Oryctolagus cuniculus
Expression system: Not provided
UniProt:
  • Canonical: P11974 (Residues: 2-531; Coverage: 100%)
Gene name: PKM
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand K 1 x K
Ligand MN 1 x MN
Ligand PYR 1 x PYR
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 83.6Å b: 109.9Å c: 146.8Å
α: 94.9° β: 93.6° γ: 112.3°
R-values:
R R work R free
0.191 not available not available
Expression system: Not provided

Quick links

Citations

24 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
23 more

8 mentions without citation

A priori prediction of adsorption isotherm parameters and chromatographic behavior in ion-exchange systems.
Ladiwala et al. (2005)
7 more