› 4r7p

X-ray diffraction
3.35Å resolution

Human UDP-glucose pyrophosphorylase isoform 1 in complex with UDP-glucose

Released:
DOI: 10.2210/pdb4r7p/pdb
PDB entry 4r7p coloured by chain, front view.
PDB entry 4r7p coloured by chain, side view.
PDB entry 4r7p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.
Führing JI, Cramer JT, Schneider J, Baruch P, Gerardy-Schahn R, Fedorov R
Sci Rep 5 9618 (2015)
PMID: 25860585

Function and Biology Details

Reaction catalysed: 
UTP + alpha-D-glucose 1-phosphate = diphosphate + UDP-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172602 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UTP--glucose-1-phosphate uridylyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 526 amino acids
Theoretical weight: 58.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16851 (Residues: 2-508; Coverage: 100%)
Gene names: UGP1, UGP2
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand UPG 1 x UPG
Ligand SO4 15 x SO4
Ligand ACT 4 x ACT
Ligand EDO 11 x EDO
Ligand ZN 11 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P3121
Unit cell:
a: 138.97Å b: 138.97Å c: 311.62Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.199 0.247
Expression system: Escherichia coli

Quick links

Citations

5 review citations

UDP-Sugar Producing Pyrophosphorylases: Distinct and Essential Enzymes With Overlapping Substrate Specificities, Providing de novo Precursors for Glycosylation Reactions.
Decker et al. (2018)
4 more

3 mentions without citation

A quaternary mechanism enables the complex biological functions of octameric human UDP-glucose pyrophosphorylase, a key enzyme in cell metabolism.
Führing et al. (2015)
2 more