› 1nhx

X-ray diffraction
2.1Å resolution

PEPCK COMPLEX WITH A GTP-COMPETITIVE INHIBITOR

Released:
DOI: 10.2210/pdb1nhx/pdb
PDB entry 1nhx coloured by chain, front view.
PDB entry 1nhx coloured by chain, side view.
PDB entry 1nhx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray structures of two xanthine inhibitors bound to PEPCK and N-3 modifications of substituted 1,8-dibenzylxanthines.
Foley LH, Wang P, Dunten P, Ramsey G, Gubler ML, Wertheimer SJ
Bioorg Med Chem Lett 13 3871-4 (2003)
PMID: 14552798

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: 69.53 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

5 bound ligands:
Ligand MN 1 x MN
Ligand NA 1 x NA
Ligand PEP 1 x PEP
Ligand FTB 1 x FTB
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 45.383Å b: 61.452Å c: 62.265Å
α: 89.71° β: 70.24° γ: 72.56°
R-values:
R R work R free
0.175 0.173 0.217
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Kinases on Double Duty: A Review of UniProtKB Annotated Bifunctionality within the Kinome.
Rangwala et al. (2022)
5 other articles

1 mention without citation

Insights into Lysine Deacetylation of Natively Folded Substrate Proteins by Sirtuins.
Knyphausen et al. (2016)