› 8j25

X-ray diffraction
2.6Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-229092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein; Protein PML Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 47.02 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 25-25, 27-392; Coverage: 99%)
  • Canonical: P29590 (Residues: 183-236; Coverage: 6%)
Gene names: JW3994, MYL, PML, PP8675, RNF71, TRIM19, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: R32
Unit cell:
a: 121.568Å b: 121.568Å c: 161.332Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.248
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Reduced Proteolipid Protein 2 promotes endoplasmic reticulum stress-related apoptosis and increases drug sensitivity in acute myeloid leukemia.
Xie et al. (2023)

1 mention without citation

Structural Basis of PML-RARA Oncoprotein Targeting by Arsenic Unravels a Cysteine Rheostat Controlling PML Body Assembly and Function.
Bercier et al. (2023)