› 7r6y

X-ray diffraction
2.25Å resolution

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 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
Molecule details ›
Chains: A, B, C, D
Length: 531 amino acids
Theoretical weight: 58.13 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P11974 (Residues: 1-531; Coverage: 100%)
Gene name: PKM
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ACT 9 x ACT
Ligand OXL 4 x OXL
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 108.34Å b: 121.83Å c: 161.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.25
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

PYK-SubstitutionOME: an integrated database containing allosteric coupling, ligand affinity and mutational, structural, pathological, bioinformatic and computational information about pyruvate kinase isozymes.
Swint-Kruse et al. (2023)

1 mention without citation

The K+-Dependent and -Independent Pyruvate Kinases Acquire the Active Conformation by Different Mechanisms.
Ramírez-Silva et al. (2022)