› 5l9q

X-ray diffraction
1.75Å resolution

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184429 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Macro domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 208 amino acids
Theoretical weight: 22.8 KDa
Source organism: Oceanobacillus iheyensis HTE831
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8EP31 (Residues: 1-185; Coverage: 100%)
Gene name: OB2288
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: P21
Unit cell:
a: 47.342Å b: 95.714Å c: 54.734Å
α: 90° β: 115.59° γ: 90°
R-values:
R R work R free
0.172 0.17 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

(ADP-ribosyl)hydrolases: structure, function, and biology.
Rack et al. (2020)
1 more

2 mentions without citation

ADP-ribosylation systems in bacteria and viruses.
Mikolčević et al. (2021)
1 more