1IDS Superoxide Dismutase date Sep 29, 1994
authors J.B.Cooper, K.Mcintyre, S.P.Wood, Y.Zhang, D.Young
compound source
Iron-Dependent Superoxide Dismutase (E.C.1.15.1.1) (Fe-Superoxide Dismutase, Fe-Sod)
Mycobacterium Tuberculosis) Recombinant Form Expressed In (Mycobacterium Vaccae)
symmetry Space Group: P 21
R_factor 0.167
crystal
cell
length a length b length c angle alpha angle beta angle gamma
68.650 85.400 66.350 90.00 99.86 90.00
method X-Ray Diffractionresolution 2.0 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
A, D, C, B
  • 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 referenceX-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions., Cooper JB, McIntyre K, Badasso MO, Wood SP, Zhang Y, Garbe TR, Young D, J Mol Biol 1995 Mar 3;246(4):531-44. PMID:7877174
    Data retrieval
  • Asymmetric unit, PDB entry: [header only] [complete with coordinates] (167 Kb) [Save to disk]
  • Biological Unit Coordinates (1ids.pdb1.gz) 130 Kb
  • CSU: Contacts of Structural Units for 1IDS
  • Likely Quarternary Molecular Structure file(s) for 1IDS
  • Structure Factors (419 Kb)
  • Retrieve 1IDS in mmCIF format [Save to disk]
  • View 1IDS 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 1IDS
  • 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 1IDS, from MSDmotif at EBI
  • Genome occurence of 1IDS's fold from GeneCensus
  • Classification of representative domains in scop (Structural Classification of Proteins)
        - Domain d1idsa1, region A:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1idsa2, region A:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1idsb1, region B:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1idsb2, region B:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1idsc1, region C:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1idsc2, region C:86-199 [Jmol] [rasmolscript] [script source]
        - Domain d1idsd1, region D:2-85 [Jmol] [rasmolscript] [script source]
        - Domain d1idsd2, region D:86-199 [Jmol] [rasmolscript] [script source]
  • Fold representative 1ids from FSSP and Dali (Families of Structurally Similar Proteins)
  • Sequence-derived information
  • View one-letter amino acid or nucleotide sequence for each chain: [1ids_C] [1ids_A] [1ids_B] [1ids_D]
  • Other resources with information on 1IDS
  • InterPro: IPR001189
  • PDBREPORT (protein verification by WHAT_CHECK procedures)
  • MMDB (Entrez's Structure Database)
  • Movements, Movies and Images
  • Domain movements in 1IDS from the Database of Macromolecular Movements.
  • 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