› 6nn5

X-ray diffraction
2.26Å resolution

The structure of human liver pyruvate kinase, hLPYK-W527H

Released:
DOI: 10.2210/pdb6nn5/pdb
PDB entry 6nn5 coloured by chain, front view.
PDB entry 6nn5 coloured by chain, side view.
PDB entry 6nn5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond.
McFarlane JS, Ronnebaum TA, Meneely KM, Chilton A, Fenton AW, Lamb AL
Acta Crystallogr F Struct Biol Commun 75 461-469 (2019)
PMID: 31204694

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKLR Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 543 amino acids
Theoretical weight: 58.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30613 (Residues: 34-574; Coverage: 94%)
  • Best match: P30613-2 (Residues: 3-543)
Gene names: PK1, PKL, PKLR
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand GOL 12 x GOL
Ligand EDO 10 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 120.01Å b: 204.624Å c: 112.376Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.264
Expression system: Escherichia coli

Quick links

Citations

2 review citations

An overview of structure, function, and regulation of pyruvate kinases.
Schormann et al. (2019)
1 more

1 mention without citation

Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation-π bond.
McFarlane et al. (2019)