› 2vgg

X-ray diffraction
2.74Å resolution

HUMAN ERYTHROCYTE PYRUVATE KINASE: R479H MUTANT

Released:
DOI: 10.2210/pdb2vgg/pdb
PDB entry 2vgg coloured by chain, front view.
PDB entry 2vgg coloured by chain, side view.
PDB entry 2vgg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.
Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A
J Biol Chem 277 23807-14 (2002)
PMID: 11960989

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: 528 amino acids
Theoretical weight: 56.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P30613 (Residues: 47-574; Coverage: 92%)
Gene names: PK1, PKL, PKLR
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand FBP 4 x FBP
Ligand PGA 4 x PGA
Ligand K 4 x K
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21
Unit cell:
a: 74.036Å b: 171.795Å c: 85.086Å
α: 90° β: 91.17° γ: 90°
R-values:
R R work R free
0.254 0.253 0.294
Expression system: Escherichia coli BL21

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Citations

9 review citations

Regulation of pyruvate metabolism and human disease.
Gray et al. (2014)
8 more