1QNN

Cambialistic superoxide dismutase from Porphyromonas gingivalis


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Crystal Structure of Cambialistic Superoxide Dismutase from Porphyromonas Gingivalis

Sugio, S.Hiraoka, B.Y.Yamakura, F.

(2000) Eur J Biochem 267: 3487

  • DOI: https://doi.org/10.1046/j.1432-1327.2000.01373.x
  • Primary Citation of Related Structures:  
    1QNN

  • PubMed Abstract: 

    The crystal structure of cambialistic superoxide dismutase (SOD) from Porphyromonas gingivalis, which exhibits full activity with either Fe or Mn at the active site, has been determined at 1.8-A resolution by molecular replacement and refined to a crystallographic R factor of 17.9% (Rfree 22.3%). The crystals belong to the space group P212121 (a = 75.5 A, b = 102.7 A, c = 99.6 A) with four identical subunits in the asymmetric unit. Each pair of subunits forms a compact dimer, but not a tetramer, with 222 point symmetry. Each subunit has 191 amino-acid residues most of which are visible in electron density maps, and consists of seven alpha helices and one three-stranded antiparallel beta sheet. The metal ion, a 3 : 1 mixture of Fe and Mn, is coordinated with five ligands (His27, His74, His161, Asp157, and water) arranged at the vertices of a trigonal bipyramid. Although the overall structural features, including the metal coordination geometry, are similar to those found in other single-metal containing SODs, P. gingivalis SOD more closely resembles the dimeric Fe-SODs from Escherichia coli rather than another cambialistic SOD from Propionibacterium shermanii, which itself is rather similar to other tetrameric SODs.


  • Organizational Affiliation

    Yokohama Research Center, Mitsubishi Chemical Corporation, Aoba, Yokohama, Japan.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SUPEROXIDE DISMUTASE
A, B, C, D
191Porphyromonas gingivalisMutation(s): 0 
EC: 1.15.1.1
UniProt
Find proteins for P19665 (Porphyromonas gingivalis (strain ATCC BAA-308 / W83))
Explore P19665 
Go to UniProtKB:  P19665
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP19665
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.80 Å
  • R-Value Free: 0.223 
  • R-Value Work: 0.179 
  • R-Value Observed: 0.179 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 75.47α = 90
b = 102.66β = 90
c = 99.59γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
PROCESSdata reduction
PROCESSdata scaling
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-06-21
    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: 2017-07-05
    Changes: Data collection
  • Version 1.4: 2019-03-06
    Changes: Data collection, Experimental preparation
  • Version 1.5: 2019-04-10
    Changes: Data collection, Source and taxonomy
  • Version 1.6: 2019-05-08
    Changes: Data collection, Experimental preparation
  • Version 1.7: 2023-12-13
    Changes: Data collection, Database references, Derived calculations, Other, Refinement description