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PDBsum entry 4b1h

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protein ligands links
Hydrolase PDB id
4b1h

 

 

 

 

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Contents
Protein chain
507 a.a.
Ligands
BME
DTV
GOL ×2
AR6 ×2
SO4 ×2
Waters ×378
PDB id:
4b1h
Name: Hydrolase
Title: Structure of human parg catalytic domain in complex with adp-ribose
Structure: Poly(adp-ribose) glycohydrolase. Chain: a. Fragment: catalytic domain, residues 448-976. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: gold.
Resolution:
2.00Å     R-factor:   0.205     R-free:   0.241
Authors: C.Brassington,J.Ellston,G.Hassall,G.Holdgate,M.Mcalister,G.Smith, J.A.Tucker,M.Watson
Key ref: J.A.Tucker et al. (2012). Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives. Plos One, 7, e50889. PubMed id: 23251397
Date:
10-Jul-12     Release date:   19-Dec-12    
PROCHECK
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 Headers
 References

Protein chain
Q86W56  (PARG_HUMAN) -  Poly(ADP-ribose) glycohydrolase from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
976 a.a.
507 a.a.*
Key:    Secondary structure
* PDB and UniProt seqs differ at 7 residue positions (black crosses)

 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    
 
 
Plos One 7:e50889 (2012)
PubMed id: 23251397  
 
 
Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives.
J.A.Tucker, N.Bennett, C.Brassington, S.T.Durant, G.Hassall, G.Holdgate, M.McAlister, J.W.Nissink, C.Truman, M.Watson.
 
  ABSTRACT  
 
No abstract given.

 

 

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