› 1khe

X-ray diffraction
2.4Å resolution

PEPCK complex with nonhydrolyzable GTP analog, MAD data

Released:
DOI: 10.2210/pdb1khe/pdb
PDB entry 1khe coloured by chain, front view.
PDB entry 1khe coloured by chain, side view.
PDB entry 1khe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human cytosolic phosphoenolpyruvate carboxykinase reveals a new GTP-binding site.
Dunten P, Belunis C, Crowther R, Hollfelder K, Kammlott U, Levin W, Michel H, Ramsey GB, Swain A, Weber D, Wertheimer SJ
J Mol Biol 316 257-64 (2002)
PMID: 11851336

Function and Biology Details

Reaction catalysed: 
GTP + oxaloacetate = GDP + phosphoenolpyruvate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152943 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoenolpyruvate carboxykinase, cytosolic [GTP] Chain: A
Molecule details ›
Chain: A
Length: 625 amino acids
Theoretical weight: 70.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P35558 (Residues: 1-622; Coverage: 100%)
Gene names: PCK1, PEPCK1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand GCP 1 x GCP
1 modified residue:
Ligand MSE 22 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P1
Unit cell:
a: 45.386Å b: 60.54Å c: 61.833Å
α: 88.36° β: 70.39° γ: 72.37°
R-values:
R R work R free
0.174 0.17 0.246
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria.
Sauer et al. (2005)
5 more

2 mentions without citation

Mixed Inhibition of cPEPCK by Genistein, Using an Extended Binding Site Located Adjacent to Its Catalytic Cleft.
Katiyar et al. (2015)
1 more