1N0J

The Structure of Human Mitochondrial MN3+ Superoxide Dismutase Reveals a Novel Tetrameric Interface of Two 4-Helix Bundles


Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
BSCOP2B SuperfamilyFe, Mn superoxide dismutase (SOD), C-terminal domain 8033672 3000916 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyFe, Mn superoxide dismutase (SOD), N-terminal domain 8033670 3000794 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFe, Mn superoxide dismutase (SOD), C-terminal domain 8033672 3000916 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyFe, Mn superoxide dismutase (SOD), N-terminal domain 8033670 3000794 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
BSod_Fe_Ne1n0jB4 A: alpha bundlesX: Long alpha-hairpinH: Fe,Mn superoxide dismutase (SOD), N-terminal domain (From Topology)T: Fe,Mn superoxide dismutase (SOD), N-terminal domainF: Sod_Fe_NECOD (1.6)
BSod_Fe_Ce1n0jB3 A: a+b three layersX: Fe,Mn superoxide dismutase (SOD)-C (From Topology)H: Fe,Mn superoxide dismutase (SOD)-C (From Topology)T: Fe,Mn superoxide dismutase (SOD)-CF: Sod_Fe_CECOD (1.6)
ASod_Fe_Ne1n0jA4 A: alpha bundlesX: Long alpha-hairpinH: Fe,Mn superoxide dismutase (SOD), N-terminal domain (From Topology)T: Fe,Mn superoxide dismutase (SOD), N-terminal domainF: Sod_Fe_NECOD (1.6)
ASod_Fe_Ce1n0jA3 A: a+b three layersX: Fe,Mn superoxide dismutase (SOD)-C (From Topology)H: Fe,Mn superoxide dismutase (SOD)-C (From Topology)T: Fe,Mn superoxide dismutase (SOD)-CF: Sod_Fe_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00081Iron/manganese superoxide dismutases, alpha-hairpin domain (Sod_Fe_N)Iron/manganese superoxide dismutases, alpha-hairpin domainsuperoxide 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 Mn/Fe-binding family is one. In humans, there is a cytopla ...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 Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. N-terminal domain is a long alpha antiparallel hairpin. A small fragment of YTRE_LEPBI matches well - sequencing error?
Domain
A, B
PF02777Iron/manganese superoxide dismutases, C-terminal domain (Sod_Fe_C)Iron/manganese superoxide dismutases, C-terminal domainsuperoxide 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 Mn/Fe-binding family is one. In humans, there is a cytoplas ...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 Mn/Fe-binding family is one. In humans, there is a cytoplasmic Cu/Zn SOD, and a mitochondrial Mn/Fe SOD. C-terminal domain is a mixed alpha/beta fold.
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
Superoxide dismutase [Mn]

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B
PharosP04179