› 7aks

X-ray diffraction
1.86Å resolution

Human ADP-ribosylserine hydrolase ARH3 mutant E41A in complex with H2B-S7-mar peptide

Released:
DOI: 10.2210/pdb7aks/pdb
PDB entry 7aks coloured by chain, front view.
PDB entry 7aks coloured by chain, side view.
PDB entry 7aks coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
Rack JGM, Liu Q, Zorzini V, Voorneveld J, Ariza A, Honarmand Ebrahimi K, Reber JM, Krassnig SC, Ahel D, van der Marel GA, Mangerich A, McCullagh JSO, Filippov DV, Ahel I
Nat Commun 12 4581 (2021)
PMID: 34321462

Function and Biology Details

Reaction catalysed: 
Hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkage of ribose-ribose bond to produce free ADP-D-ribose
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-167996 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ADP-ribosylhydrolase ARH3 Chains: AAA, CCC, EEE, GGG
Molecule details ›
Chains: AAA, CCC, EEE, GGG
Length: 349 amino acids
Theoretical weight: 37.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NX46 (Residues: 19-363; Coverage: 95%)
Gene names: ADPRHL2, ADPRS, ARH3
Sequence domains: ADP-ribosylglycohydrolase
modified peptide Chains: BaB, DaD, FaF, HaH
Molecule details ›
Chains: BaB, DaD, FaF, HaH
Length: 11 amino acids
Theoretical weight: 1.1 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

4 bound ligands:
Ligand MG 9 x MG
Ligand EDO 19 x EDO
Ligand ACT 28 x ACT
Ligand AR6 4 x AR6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P21212
Unit cell:
a: 123.36Å b: 158.638Å c: 74.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.195
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

10 review citations

ADP-Ribosylation as Post-Translational Modification of Proteins: Use of Inhibitors in Cancer Control.
Poltronieri et al. (2021)
9 more

3 mentions without citation

ADP-ribosylation from molecular mechanisms to therapeutic implications.
Suskiewicz et al. (2023)
2 more