› 1vhu

X-ray diffraction
1.34Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128057 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribose glycohydrolase AF_1521 Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 23.53 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28751 (Residues: 1-192; Coverage: 100%)
Gene name: AF_1521
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1

Ligands and Environments

1 bound ligand:
Ligand MES 1 x MES
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21212
Unit cell:
a: 54.57Å b: 60.966Å c: 52.746Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 0.18
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

4 mentions without citation

ADP-ribose-1"-monophosphatase: a conserved coronavirus enzyme that is dispensable for viral replication in tissue culture.
Putics et al. (2005)
3 more