› 1aqf

X-ray diffraction
2.7Å resolution

PYRUVATE KINASE FROM RABBIT MUSCLE WITH MG, K, AND L-PHOSPHOLACTATE

Released:
DOI: 10.2210/pdb1aqf/pdb
PDB entry 1aqf coloured by chain, front view.
PDB entry 1aqf coloured by chain, side view.
PDB entry 1aqf coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Ligand-induced domain movement in pyruvate kinase: structure of the enzyme from rabbit muscle with Mg2+, K+, and L-phospholactate at 2.7 A resolution.
Larsen TM, Benning MM, Wesenberg GE, Rayment I, Reed GH
Arch Biochem Biophys 345 199-206 (1997)
PMID: 9308890

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:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 530 amino acids
Theoretical weight: 58 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P11974 (Residues: 2-531; Coverage: 100%)
Gene name: PKM
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand K 8 x K
Ligand MG 8 x MG
Ligand PEQ 8 x PEQ
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 144.4Å b: 112.6Å c: 171.2Å
α: 90° β: 93.7° γ: 90°
R-values:
R R work R free
0.196 0.196 not available

Quick links

Citations

6 review citations

NMR studies of protein structure and dynamics.
Kay LE. (2005)
5 more

6 mentions without citation

A Molecular Dynamics Study of Allosteric Transitions in Leishmania mexicana Pyruvate Kinase.
Naithani et al. (2015)
5 more