Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
SO4 Sulfate ion
ZN Zinc ion
Non-standard Residues
Code Name Show
CSX S-oxy cysteine
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1P1V   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Crystal Structure of FALS-associated human Copper-Zinc Superoxide Dismutase (CuZnSOD) Mutant D125H to 1.4A
Release Data : 2003-08-26
Compound :
mol_id molecule chains
1 Superoxide dismutase [Cu-Zn] A,B,C
ec: 1.15.1.1
mutation: D125H
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Saccharomyces cerevisiae  (taxid:4932)
gene: SOD1
expression_system_common: Baker's yeast
expression_system_strain: EG118
expression_system_vector_type: plasmid
expression_system_plasmid: YEp351
Authors : Elam, J.S., Malek, K., Rodriguez, J.A., Doucette, P.A., Taylor, A.B., Hayward, L.J., Cabelli, D.E., Valentine, J.S., Hart, P.J.
Keywords : beta-barrel, bound anion at copper site, CuZnSOD peroxidation mechanism, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 1.40 Å )
Citation :

An Alternative Mechanism of Bicarbonate-mediated Peroxidation by Copper-Zinc Superoxide Dismutase: RATES ENHANCED VIA PROPOSED ENZYME-ASSOCIATED PEROXYCARBONATE INTERMEDIATE

Elam, J.S.,Malek, K.,Rodriguez, J.A.  et al.
(2003)  J.Biol.Chem.  278 : 21032 - 21039

PubMed: 12649272
DOI: 10.1074/jbc.M300484200

Chain : A, B, C
UniProt : P00441 (SODC_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
2 H(+) + 2 superoxide = H2O2 + O2 1.15.1.1 PubMed:24140062
-