1MML

MECHANISTIC IMPLICATIONS FROM THE STRUCTURE OF A CATALYTIC FRAGMENT OF MMLV REVERSE TRANSCRIPTASE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.257 
  • R-Value Observed: 0.198 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase.

Georgiadis, M.M.Jessen, S.M.Ogata, C.M.Telesnitsky, A.Goff, S.P.Hendrickson, W.A.

(1995) Structure 3: 879-892

  • DOI: https://doi.org/10.1016/S0969-2126(01)00223-4
  • Primary Citation of Related Structures:  
    1MML

  • PubMed Abstract: 

    Reverse transcriptase (RT) converts the single-stranded RNA genome of a retrovirus into a double-stranded DNA copy for integration into the host genome. This process requires ribonuclease H as well as RNA- and DNA-directed DNA polymerase activities. Although the overall organization of HIV-1 RT is known from previously reported crystal structures, no structure of a complex including a metal ion, which is essential for its catalytic activity, has been reported.


  • Organizational Affiliation

    Waksman Institute, Rutgers University, Piscataway, NJ 08855, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
MMLV REVERSE TRANSCRIPTASE265Moloney murine leukemia virusMutation(s): 0 
Gene Names: MMLV-RT
UniProt
Find proteins for P03355 (Moloney murine leukemia virus (isolate Shinnick))
Explore P03355 
Go to UniProtKB:  P03355
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03355
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.257 
  • R-Value Observed: 0.198 
  • Space Group: P 32 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.1α = 90
b = 84.1β = 90
c = 74γ = 120
Software Package:
Software NamePurpose
PROLSQrefinement
DENZOdata reduction

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-10-15
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-14
    Changes: Data collection, Database references, Other