› 1a5u

X-ray diffraction
2.35Å resolution

PYRUVATE KINASE COMPLEX WITH BIS MG-ATP-NA-OXALATE

Released:
DOI: 10.2210/pdb1a5u/pdb
PDB entry 1a5u coloured by chain, front view.
PDB entry 1a5u coloured by chain, side view.
PDB entry 1a5u coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel.
Larsen TM, Benning MM, Rayment I, Reed GH
Biochemistry 37 6247-55 (1998)
PMID: 9572839

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-146016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyruvate kinase PKM Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 530 amino acids
Theoretical weight: 58 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P11974 (Residues: 2-531; Coverage: 100%)
Gene name: PKM
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand NA 8 x NA
Ligand OXL 8 x OXL
Ligand MG 14 x MG
Ligand ATP 6 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 95.3Å b: 216.5Å c: 258.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available

Quick links

Citations

8 review citations

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

3 mentions without citation

On the molecular discrimination between adenine and guanine by proteins.
Nobeli et al. (2001)
2 more