2CDY

Manganese Superoxide Dismutase (Mn-SOD) from Deinococcus radiodurans


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.176 

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This is version 1.4 of the entry. See complete history


Literature

Structure of the manganese superoxide dismutase from Deinococcus radiodurans in two crystal forms.

Dennis, R.J.Micossi, E.McCarthy, J.Moe, E.Gordon, E.J.Kozielski-Stuhrmann, S.Leonard, G.A.McSweeney, S.

(2006) Acta Crystallogr Sect F Struct Biol Cryst Commun 62: 325-329

  • DOI: https://doi.org/10.1107/S1744309106008402
  • Primary Citation of Related Structures:  
    2CDY, 2CE4

  • PubMed Abstract: 

    The structure of the manganese superoxide dismutase (Mn-SOD; DR1279) from Deinococcus radiodurans has been determined in two different crystal forms. Both crystal forms are monoclinic with space group P2(1). Form I has unit-cell parameters a = 44.28, b = 83.21, c = 59.52 angstroms, beta = 110.18 degrees and contains a homodimer in the asymmetric unit, with structure refinement (R = 16.8%, R(free) = 23.6%) carried out using data to d(min) = 2.2 angstroms. Form II has unit-cell parameters a = 43.57, b = 87.10, c = 116.42 angstroms, beta = 92.1 degrees and an asymmetric unit containing two Mn-SOD homodimers; structure refinement was effected to a resolution of 2.0 angstroms (R = 17.2%, R(free) = 22.3%). The resulting structures are compared with that of Mn-SOD from Escherichia coli, with which they are shown to be essentially isostructural.


  • Organizational Affiliation

    Macromolecular Crystallography Group, European Synchrotron Radiation Facility, 38043 Grenoble CEDEX 9, France.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUPEROXIDE DISMUTASE [MN]
A, B, C, D
231Deinococcus radiodurans R1 = ATCC 13939 = DSM 20539Mutation(s): 0 
EC: 1.15.1.1
UniProt
Find proteins for Q9RUV2 (Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1))
Explore Q9RUV2 
Go to UniProtKB:  Q9RUV2
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9RUV2
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.221 
  • R-Value Work: 0.173 
  • R-Value Observed: 0.176 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 43.577α = 90
b = 87.1β = 92.1
c = 116.418γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-02-13
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2018-02-28
    Changes: Database references, Source and taxonomy, Structure summary
  • Version 1.4: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description