› 1pkm

X-ray diffraction
2.6Å resolution

THE REFINED THREE-DIMENSIONAL STRUCTURE OF CAT MUSCLE (M1) PYRUVATE KINASE, AT A RESOLUTION OF 2.6 ANGSTROMS

Released:
DOI: 10.2210/pdb1pkm/pdb
PDB entry 1pkm coloured by chain, front view.
PDB entry 1pkm coloured by chain, side view.
PDB entry 1pkm coloured by chain, top view.
Source organism: Felis catus
Primary publication:
Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at a resolution of 2.6 A.
Allen SC, Muirhead H
Acta Crystallogr D Biol Crystallogr 52 499-504 (1996)
PMID: 15299671

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-146021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 58 KDa
Source organism: Felis catus
UniProt:
  • Canonical: P11979 (Residues: 2-531; Coverage: 100%)
Gene names: PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I222
Unit cell:
a: 88.4Å b: 115.3Å c: 131Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.175 not available

Quick links

Citations

3 review citations

Triosephosphate isomerase: a highly evolved biocatalyst.
Wierenga et al. (2010)
2 more

4 mentions without citation

Sialidase-like Asp-boxes: sequence-similar structures within different protein folds.
Copley et al. (2001)
3 more