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PDBsum entry 2b6a
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* Residue conservation analysis
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PDB id:
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Transferase
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Title:
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Crystal structure of HIV-1 reverse transcriptase (rt) in complex with thr-50
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Structure:
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Reverse transcriptase p66 subunit. Chain: a. Fragment: residues 599-1158. Synonym: HIV-1 rt. Engineered: yes. Mutation: yes. Reverse transcriptase p51 subunit. Chain: b. Fragment: residues 599-1028.
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Source:
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Human immunodeficiency virus 1. Organism_taxid: 11676. Gene: pol. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Dimer (from
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Resolution:
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2.65Å
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R-factor:
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0.226
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R-free:
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0.277
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Authors:
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M.L.Morningstar,T.Roth,M.K.Smith,M.Zajac,K.Watson,R.W.Buckheit,K.Das, W.Zhang,E.Arnold,C.J.Michejda
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Key ref:
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M.L.Morningstar
et al.
Crystal structure of HIV-1 reverse transcriptase (rt) in complex with thr-50.
To be published,
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Date:
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30-Sep-05
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Release date:
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01-Nov-05
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PROCHECK
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Headers
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References
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Enzyme class 1:
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Chains A, B:
E.C.2.7.7.-
- ?????
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Enzyme class 2:
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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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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 3:
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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 4:
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Chains A, B:
E.C.3.1.-.-
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Enzyme class 5:
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Chains A, B:
E.C.3.1.13.2
- exoribonuclease H.
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Reaction:
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Exonucleolytic cleavage to 5'-phosphomonoester oligonucleotides in both 5'- to 3'- and 3'- to 5'-directions.
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Enzyme class 6:
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Chains A, B:
E.C.3.1.26.13
- retroviral ribonuclease H.
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Enzyme class 7:
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Chains A, B:
E.C.3.4.23.16
- HIV-1 retropepsin.
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Reaction:
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Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
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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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