› 4ip7

X-ray diffraction
1.8Å resolution

Structure of the S12D variant of human liver pyruvate kinase in complex with citrate and FBP.

Released:
DOI: 10.2210/pdb4ip7/pdb
Model geometry
Fit model/data
PDB entry 4ip7 coloured by chain, front view.
PDB entry 4ip7 coloured by chain, side view.
PDB entry 4ip7 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Energetic coupling between an oxidizable cysteine and the phosphorylatable N-terminus of human liver pyruvate kinase.
Holyoak T, Zhang B, Deng J, Tang Q, Prasannan CB, Fenton AW
Biochemistry 52 466-76 (2013)
PMID: 23270483

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: 58.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30613 (Residues: 34-574; Coverage: 94%)
  • Best match: P30613-2 (Residues: 1-543)
Gene names: PK1, PKL, PKLR
Sequence domains:
Structure domains:

Ligands and Environments

8 bound ligands:
Ligand MN 4 x MN
Ligand FLC 4 x FLC
Ligand FBP 4 x FBP
Ligand EDO 9 x EDO
Ligand PEG 2 x PEG
Ligand NA 4 x NA
Ligand 1PE 2 x 1PE
Ligand ADN 1 x ADN
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21
Unit cell:
a: 78.14Å b: 205.078Å c: 83.91Å
α: 90° β: 92.15° γ: 90°
R-values:
R R work R free
0.189 0.187 0.226
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The Nrf2 regulatory network provides an interface between redox and intermediary metabolism.
Hayes et al. (2014)
2 more

6 mentions without citation

Exploring the limits of the usefulness of mutagenesis in studies of allosteric mechanisms.
Tang et al. (2017)
5 more