Function and Biology Details
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
ADP-ribose glycohydrolase OARD1 (preferred)
PDBe Complex ID:
PDB-CPX-195256 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribose glycohydrolase OARD1
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 16.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Length: 151 amino acids
Theoretical weight: 16.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9Y530 (Residues: 3-152; Coverage: 99%)
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Ligands and Environments
1 bound ligand:
No modified residues
Experiments and Validation Details
Chemical shift assignment:
92%
Refinement method:
AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT., torsion angle dynamics, AUTOMATED METHODS WERE USED FOR BACKBONE CHEMICAL SHIFT ASSIGNMENT AND ITERATIVE NOE REFINEMENT. FINAL STRUCTURES WERE OBTAINED BY MOLECULAR DYNAMICS IN EXPLICIT SOLVENT
Expression system: Escherichia coli
