› 2g50

X-ray diffraction
1.65Å resolution

The location of the allosteric amino acid binding site of muscle pyruvate kinase.

Released:
DOI: 10.2210/pdb2g50/pdb
PDB entry 2g50 coloured by chain, front view.
PDB entry 2g50 coloured by chain, side view.
PDB entry 2g50 coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Differentiating a ligand's chemical requirements for allosteric interactions from those for protein binding. Phenylalanine inhibition of pyruvate kinase.
Williams R, Holyoak T, McDonald G, Gui C, Fenton AW
Biochemistry 45 5421-9 (2006)
PMID: 16634623

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: 57.97 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P11974 (Residues: 2-531; Coverage: 100%)
Gene name: PKM
Sequence domains:
Structure domains:

Ligands and Environments

8 bound ligands:
Ligand MN 8 x MN
Ligand K 8 x K
Ligand NA 12 x NA
Ligand ALA 8 x ALA
Ligand PYR 8 x PYR
Ligand EDO 29 x EDO
Ligand GOL 28 x GOL
Ligand ETE 1 x ETE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P1
Unit cell:
a: 82.626Å b: 109.014Å c: 144.463Å
α: 95.15° β: 93.45° γ: 112.26°
R-values:
R R work R free
0.149 0.148 0.174

Quick links

Citations

10 review citations

PKM2, cancer metabolism, and the road ahead.
Dayton et al. (2016)
9 more

16 mentions without citation

Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates.
Lee JC. (2008)
15 more