› 1t5a

X-ray diffraction
2.8Å resolution

Human Pyruvate Kinase M2

Released:
DOI: 10.2210/pdb1t5a/pdb
PDB entry 1t5a coloured by chain, front view.
PDB entry 1t5a coloured by chain, side view.
PDB entry 1t5a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for tumor pyruvate kinase M2 allosteric regulation and catalysis.
Dombrauckas JD, Santarsiero BD, Mesecar AD
Biochemistry 44 9417-29 (2005)
PMID: 15996096

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-146985 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 567 amino acids
Theoretical weight: 62.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14618 (Residues: 1-531; Coverage: 100%)
Gene names: OIP3, PK2, PK3, PKM, PKM2
Sequence domains:
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand FBP 4 x FBP
Ligand OXL 4 x OXL
Ligand PO4 4 x PO4
Ligand MG 4 x MG
Ligand K 4 x K
Ligand GOL 20 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 108.209Å b: 145.006Å c: 159.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.231 0.278
Expression system: Escherichia coli

Quick links

Citations

58 review citations

Tumor glycolysis as a target for cancer therapy: progress and prospects.
Ganapathy-Kanniappan et al. (2013)
57 more

30 mentions without citation

Human pyruvate kinase M2: a multifunctional protein.
Gupta et al. (2010)
29 more