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PDBsum entry 4e7h
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Recombination/DNA
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PDB id
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4e7h
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PDB id:
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| Name: |
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Recombination/DNA
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Title:
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Pfv intasome prior to 3'-processing, apo form (ui-apo)
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Structure:
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Pro-pol polyprotein. Chain: a, b. Fragment: unp residues 752-1143. Synonym: pr125pol, protease/reverse transcriptase/ribonuclease h, p87pro-rt-rnaseh, protease/reverse transcriptase, p65pro-rt, ribonuclease h, rnase h, integrase, in, p42in. Ec: 2.7.7.49, 2.7.7.7, 3.1.26.4, 3.4.23.-. Engineered: yes. DNA (5'-
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Source:
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Human spumaretrovirus. Sfvcpz(hu). Organism_taxid: 11963. Strain: hsrv2. Gene: pol. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic DNA.
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Resolution:
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2.57Å
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R-factor:
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0.188
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R-free:
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0.219
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Authors:
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S.Hare,P.Cherepanov
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Key ref:
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S.Hare
et al.
(2012).
3'-processing and strand transfer catalysed by retroviral integrase in crystallo.
Embo J,
31,
3020-3028.
PubMed id:
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Date:
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17-Mar-12
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Release date:
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23-May-12
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PROCHECK
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Headers
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References
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Enzyme class 2:
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Chains A, B:
E.C.2.7.7.-
- ?????
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Enzyme class 3:
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Chains A, B:
E.C.2.7.7.49
- RNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Enzyme class 4:
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Chains A, B:
E.C.2.7.7.7
- DNA-directed Dna polymerase.
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Reaction:
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DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
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DNA(n)
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+
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2'-deoxyribonucleoside 5'-triphosphate
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=
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DNA(n+1)
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+
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diphosphate
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Enzyme class 5:
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Chains A, B:
E.C.3.1.-.-
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Enzyme class 6:
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Chains A, B:
E.C.3.1.26.4
- ribonuclease H.
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Reaction:
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Endonucleolytic cleavage to 5'-phosphomonoester.
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Enzyme class 7:
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Chains A, B:
E.C.3.4.23.-
- ?????
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Note, where more than one E.C. class is given (as above), each may
correspond to a different protein domain or, in the case of polyprotein
precursors, to a different mature protein.
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Embo J
31:3020-3028
(2012)
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PubMed id:
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3'-processing and strand transfer catalysed by retroviral integrase in crystallo.
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S.Hare,
G.N.Maertens,
P.Cherepanov.
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ABSTRACT
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');
}
}
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