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PDBsum entry 4b1h
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PDB id:
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Hydrolase
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Title:
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Structure of human parg catalytic domain in complex with adp-ribose
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Structure:
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Poly(adp-ribose) glycohydrolase. Chain: a. Fragment: catalytic domain, residues 448-976. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: gold.
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Resolution:
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2.00Å
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R-factor:
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0.205
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R-free:
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0.241
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Authors:
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C.Brassington,J.Ellston,G.Hassall,G.Holdgate,M.Mcalister,G.Smith, J.A.Tucker,M.Watson
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Key ref:
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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:
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Date:
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10-Jul-12
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Release date:
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19-Dec-12
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PROCHECK
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Headers
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References
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Q86W56
(PARG_HUMAN) -
Poly(ADP-ribose) glycohydrolase from Homo sapiens
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Seq: Struc:
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976 a.a.
507 a.a.*
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Key: |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 7 residue positions (black
crosses)
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Enzyme class:
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E.C.3.2.1.143
- poly(ADP-ribose) glycohydrolase.
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Pathway:
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Poly(ADP-ribose) Glycohydrolase
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Reaction:
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[(1''->2')-ADP-alpha-D-ribose](n) + H2O = [(1''->2')-ADP-alpha-D- ribose](n-1) + ADP-D-ribose
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[(1''->2')-ADP-alpha-D-ribose](n)
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+
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H2O
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=
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[(1''->2')-ADP-alpha-D- ribose](n-1)
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+
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ADP-D-ribose
Bound ligand (Het Group name = )
corresponds exactly
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Plos One
7:e50889
(2012)
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PubMed id:
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Structures of the human poly (ADP-ribose) glycohydrolase catalytic domain confirm catalytic mechanism and explain inhibition by ADP-HPD derivatives.
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J.A.Tucker,
N.Bennett,
C.Brassington,
S.T.Durant,
G.Hassall,
G.Holdgate,
M.McAlister,
J.W.Nissink,
C.Truman,
M.Watson.
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ABSTRACT
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');
}
}
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