› 8dbm

Electron Microscopy
2.4Å resolution

Human PRPS1 with Phosphate and PRPP; Filament Interface

Released:
DOI: 10.2210/pdb8dbm/pdb
PDB entry 8dbm coloured by chain, front view.
PDB entry 8dbm coloured by chain, side view.
PDB entry 8dbm 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-27290

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 dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158118 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-phosphate pyrophosphokinase 1 Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 318 amino acids
Theoretical weight: 34.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60891 (Residues: 2-318; Coverage: 100%)
Gene name: PRPS1
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand PRP 12 x PRP
Ligand PO4 12 x PO4
Ligand MG 24 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.4Å
Relevant EMDB volumes: EMD-27290
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)
6 other articles

1 mention without citation

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