1GN2 Oxidoreductase date Oct 02, 2001
title S123c Mutant Of The Iron-Superoxide Dismutase From Mycobacterium Tuberculosis.
authors K.A.Bunting, J.B.Cooper, I.J.Tickle, D.B.Young
compound source
Molecule: Superoxide Dismutase
Chain: A, B, C, D, E, F, G, H
Ec: 1.15.1.1
Engineered: Yes
Mutation: Yes
Organism_scientific: Mycobacterium Tuberculosis
Expression_system: Mycobacterium Vaccae
symmetry Space Group: P 1 21 1
R_factor 0.249
crystal
cell
length a length b length c angle alpha angle beta angle gamma
103.080 106.330 76.100 90.00 92.37 90.00
method X-Ray Diffractionresolution 3.4 Å
ligand FE enzyme Superoxide dismutase;. Superoxidase dismutase;. Copper-zinc superoxide dismutase;. Cu-Zn superoxide dismutase;. Ferrisuperoxide dismutase;. Superoxide dismutase I;. Superoxide dismutase II;. SOD;. Cu,Zn-SOD;. Mn-SOD;. Fe-SOD;. SODF;. SODS;. SOD-1;. SOD-2;. SOD-3;. SOD-4;. Hemocuprein;. Erythrocuprein;. Cytocuprein;. Cuprein;. Hepatocuprein. Oxidoreductase E.C.1.15.1.1 BRENDA
similarity Belongs to the iron/manganese superoxide dismutase family.[Sod_Fe_C]
subunit Homotetramer.
catalytic activ. 2 superoxide + 2 h(+) = o(2) + h(2)o(2).
subcellular loc. Secreted protein.
genes sodB (A. fumigatus); SOD1 (B. taurus); sodA (D. radiodurans); sodA, sodB, sodC (E. coli); SOD1, SOD2 (H. sapiens); sod (M. thermoautotrophicum); MT0447, sodC (M. tuberculosis); sodC (P. leiognathi); sodB (P. gingivalis); sodA (P. freudenreichii); sodB (P. putida); sod (P. aerophilum); sodC1, sodC (S. typhimurium); SOD (S. mansoni); SODCP (S. oleracea); sodN (S. seoulensis); sod (S. acidocaldarius); sod (S. solfataricus); sodA (T. thermophilus); sod1-B (X. laevis); SOD1 (S. cerevisiae)
function Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Gene
Ontology
ChainFunctionProcessComponent
F, A, E, B, H, C, D, G
  • superoxide dismutase activit...
  • iron ion binding
  • oxidoreductase activity
  • metal ion binding
  • superoxide metabolic process...

  • disease Amyotrophic lateral sclerosis,due to SOD1 deficiency
    Superoxide Dismutase 2; Sod2
    Primary referenceEngineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis., Bunting KA, Cooper JB, Tickle IJ, Young DB, Arch Biochem Biophys 2002 Jan 1;397(1):69-76. PMID:11747311
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (247 Kb) [Save to disk]
  • Biological Unit Coordinates (1gn2.pdb1.gz) 216 Kb
  • CSU: Contacts of Structural Units for 1GN2
  • Likely Quarternary Molecular Structure file(s) for 1GN2
  • Structure Factors (220 Kb)
  • Retrieve 1GN2 in mmCIF format [Save to disk]
  • View 1GN2 in 3D
  • On Jmol, a nice Rasmol like molecule viewer. This is good for easiest viewing of basic structure.
  • On FirstGlance, an excellent tool for a guided tour on the structure components, by E. Martz.
  • On AstexViewer, from MSD-EBI (viewer documentation).
  • On RasMol (Install RasMol freeware) Here's help on how to use RasMol.
  • Visual 3D analysis of 1GN2
  • Protein Explorer, Easier to use and more powerful than RasMol. (Win and Mac only)
  • Noncovalent Bond Finder displays the closest contacts to ligand or interface, reports distances, walks over water bridges.
  • STING, shows the sequence and maps the locations of sequence residues or residue ranges onto the 3D structure.
  • GRASS (Graphical Representation and Analysis of Structure Server)
  • Cartoon representation from PDB Cartoon
  • Ramachandran plot from PDBSum
  • Structure-derived information
  • Dipole moment, from Dipole Server at Weizmann Institute
  • Crystal Contacts, from CryCo at Weizmann Institute
  • 3D motif for 1GN2, from MSDmotif at EBI
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1gn2a1, region A:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2a2, region A:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2b1, region B:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2b2, region B:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2c1, region C:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2c2, region C:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2d1, region D:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2d2, region D:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2e1, region E:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2e2, region E:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2f1, region F:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2f2, region F:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2g1, region G:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2g2, region G:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2h1, region H:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1gn2h2, region H:86-199 [Jmol] [rasmolscript] [script source]
  • Fold representative 1gn2 from FSSP and Dali (Families of Structurally Similar Proteins)
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1gn2_E] [1gn2_H] [1gn2_A] [1gn2_B] [1gn2_C] [1gn2_D] [1gn2_F] [1gn2_G]
  • Other resources with information on 1GN2
  • InterPro: IPR001189
  • PDBREPORT (protein verification by WHAT_CHECK procedures)
  • MMDB (Entrez's Structure Database)
  • Movements, Movies and Images
  • Images from IMB Jena Image Library of Biological Macromolecules.

  • You may enter another PDB ID code
    Go [Back], to the [PDB Lite page], to the [OCA Search page] or to the [PDB Home page]
    OCA© by Jaime Prilusky, 1996-2006
    Bioinformatics and Biological Computing
    Weizmann Institute of Science