› 3s5j

X-ray diffraction
2.02Å resolution

2.0A Crystal structure of human phosphoribosyl pyrophosphate synthetase 1

Released:
DOI: 10.2210/pdb3s5j/pdb
PDB entry 3s5j coloured by chain, front view.
PDB entry 3s5j coloured by chain, side view.
PDB entry 3s5j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal and EM structures of human phosphoribosyl pyrophosphate synthase I (PRS1) provide novel insights into the disease-associated mutations.
Chen P, Liu Z, Wang X, Peng J, Sun Q, Li J, Wang M, Niu L, Zhang Z, Cai G, Teng M, Li X
PLoS One 10 e0120304 (2015)
PMID: 25781187

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158119 (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: 35.95 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

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: R3
Unit cell:
a: 170.536Å b: 170.536Å c: 61.778Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.215 0.256
Expression system: Escherichia coli

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Citations

2 review citations

Contribution of Model Organisms to Investigating the Far-Reaching Consequences of PRPP Metabolism on Human Health and Well-Being.
Ugbogu et al. (2022)
1 more

5 mentions without citation

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