› 8dbe

Electron Microscopy
2.1Å resolution

Human PRPS1 with ADP; Hexamer

Released:
DOI: 10.2210/pdb8dbe/pdb
PDB entry 8dbe coloured by chain, front view.
PDB entry 8dbe coloured by chain, side view.
PDB entry 8dbe coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human PRPS1 filaments stabilize allosteric sites to regulate activity.
Hvorecny KL, Hargett K, Quispe JD, Kollman JM
Nat Struct Mol Biol (2023)
PMID: 36747094
Related structures: EMD-27281

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, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 318 amino acids
Theoretical weight: 34.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60891 (Residues: 1-318; Coverage: 100%)
Gene name: PRPS1
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand HSX 6 x HSX
Ligand ADP 12 x ADP
Ligand MG 12 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.1Å
Relevant EMDB volumes: EMD-27281
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Greater than the sum of parts: Mechanisms of metabolic regulation by enzyme filaments.
Hvorecny et al. (2023)
5 other articles

2 mentions without citation

Human PRPS1 filaments stabilize allosteric sites to regulate activity.
Hvorecny et al. (2023)
1 more