› 4f8e

X-ray diffraction
2.27Å resolution

Crystal structure of human PRS1 D52H mutant

Released:
DOI: 10.2210/pdb4f8e/pdb
PDB entry 4f8e coloured by chain, front view.
PDB entry 4f8e coloured by chain, side view.
PDB entry 4f8e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A small disturbance, but a serious disease: the possible mechanism of D52H-mutant of human PRS1 that causes gout.
Chen P, Li J, Ma J, Teng M, Li X
IUBMB Life 65 518-25 (2013)
PMID: 23509005

Function and Biology Details

Reaction catalysed: 
ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose 1-diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158121 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-phosphate pyrophosphokinase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 326 amino acids
Theoretical weight: 35.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60891 (Residues: 1-318; Coverage: 100%)
Gene name: PRPS1
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

2 bound ligands:
Ligand SO4 6 x SO4
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: R3
Unit cell:
a: 170.31Å b: 170.31Å c: 61.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.232
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Association of PRPS1 Mutations with Disease Phenotypes.
Mittal et al. (2015)
3 more

2 mentions without citation

Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.
Hove-Jensen et al. (2017)
1 more