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PDBsum entry 7l9h

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protein ligands metals Protein-protein interface(s) links
Hydrolase PDB id
7l9h

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
336 a.a.
Ligands
AR6 ×4
Metals
_MG ×4
Waters ×909
PDB id:
7l9h
Name: Hydrolase
Title: Crystal structure of human arh3-d77a bound to magnesium and adp-ribose
Structure: Adp-ribose glycohydrolase arh3. Chain: c, d, a, b. Synonym: adp-ribosylhydrolase 3,o-acetyl-adp-ribose deacetylase arh3, poly(adp-ribose) glycohydrolase arh3,[protein adp-ribosylarginine] hydrolase-like protein 2,[protein adp-ribosylserine] hydrolase. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: adprs, adprhl2, arh3. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.85Å     R-factor:   0.183     R-free:   0.227
Authors: Y.Pourfarjam,I.Kurinov,J.Moss,I.K.Kim
Key ref: y.pourfarjam et al. (2021). Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 (ARH3) reveals the basis of metal selectivity and different roles for the two Mg ions. J.Biol.Chem., 0, 100692-100692. PubMed id: 33894202
Date:
04-Jan-21     Release date:   28-Apr-21    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9NX46  (ARHL2_HUMAN) -  ADP-ribosylhydrolase ARH3 from Homo sapiens
Seq:
Struc:
363 a.a.
336 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.143  - poly(ADP-ribose) glycohydrolase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Poly(ADP-ribose) Glycohydrolase
      Reaction: [(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D- ribose](n-1) + ADP-D-ribose
[(1''->2')-ADP-alpha-D-ribose](n)
+ H2O
= [(1''->2')-ADP-alpha-D- ribose](n-1)
+
ADP-D-ribose
Bound ligand (Het Group name = AR6)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
J.Biol.Chem. 0:100692-100692 (2021)
PubMed id: 33894202  
 
 
Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 (ARH3) reveals the basis of metal selectivity and different roles for the two Mg ions.
y.pourfarjam, z.ma, i.kurinov, j.moss, i.k.kim.
 
  ABSTRACT  
 
No abstract given.

 

 

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