Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad2jcwa_ All beta proteins Immunoglobulin-like beta-sandwich Cu,Zn superoxide dismutase-like Cu,Zn superoxide dismutase-like Cu,Zn superoxide dismutase, SOD (Saccharomyces cerevisiae ) [TaxId: 4932 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyCu, Zn superoxide dismutase-like 8055259 3002059 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ASod_Cue2jcwA1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: Immunoglobulin-relatedT: Cu,Zn superoxide dismutase-likeF: Sod_CuECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A2.60.40.200 Mainly Beta Sandwich Immunoglobulin-like Superoxide dismutase, copper/zinc binding domainCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00080Copper/zinc superoxide dismutase (SODC) (Sod_Cu)Copper/zinc superoxide dismutase (SODC)superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SO ...superoxide dismutases (SODs) catalyse the conversion of superoxide radicals to hydrogen peroxide and molecular oxygen. Three evolutionarily distinct families of SODs are known, of which the copper/zinc-binding family is one. Defects in the human SOD1 gene cause familial amyotrophic lateral sclerosis (Lou Gehrig's disease). Structure is an eight-stranded beta sandwich, similar to the immunoglobulin fold.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
CU/ZN SUPEROXIDE DISMUTASE

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
superoxide dismutase  M-CSA #138

Copper-zinc superoxide dimutase (CuZnSOD) catalyses the disproportionation of superoxide into dioxygen and hydrogen peroxide.

In higher organisms, superoxide anions are produced as an occasional byproduct during the one-electron reduction of dioxygen in respiration and photosynthesis. Superoxides are also produced by macrophages as a part of the immune response. Excess amounts of superoxides can inactivate enzymes with iron-sulphur clusters and can lead to the formation of highly oxidising species that can damage cellular constituents. Therefore, organisms must have ways to regulate the concentration of superoxide concentrations. Many Gram-negative bacterial pathogens also possess CuZnSOD to counteract the phagocyte superoxide burst from their hosts.

Defined by 8 residues: HIS:A-46HIS:A-48HIS:A-63HIS:A-71HIS:A-80ASP:A-83HIS:A-120ARG:A-143
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