› 1f3x

X-ray diffraction
2.8Å resolution

S402P MUTANT OF RABBIT MUSCLE PYRUVATE KINASE

Released:
DOI: 10.2210/pdb1f3x/pdb
PDB 1f3x coloured by chain and viewed from the front.
PDB 1f3x coloured by chain and viewed from the side.
PDB 1f3x coloured by chain and viewed from the top.
Source organism: Oryctolagus cuniculus
Primary publication:
Structural and functional linkages between subunit interfaces in mammalian pyruvate kinase.
Wooll JO, Friesen RH, White MA, Watowich SJ, Fox RO, Lee JC, Czerwinski EW
J Mol Biol 312 525-40 (2001)
PMID: 11563914

Function and Biology Details

Reaction catalysed: 
ATP + pyruvate = ADP + phosphoenolpyruvate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (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: 57.99 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11974 (Residues: 2-531; Coverage: 100%)
Gene name: PKM
Sequence domains: Pyruvate kinase, alpha/beta domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand K 8 x K
Ligand MN 8 x MN
Ligand PYR 8 x PYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P1
Unit cell:
a: 82.138Å b: 108.707Å c: 144.387Å
α: 95.26° β: 93.47° γ: 112.24°
R-values:
R R work R free
0.241 0.241 0.27
Expression system: Escherichia coli

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Citations

1 review citation

Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates.
Lee JC. (2008)
25 other articles