1F1A

Crystal structure of yeast H48Q cuznsod fals mutant analog

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1f1aa_	All beta proteins	Immunoglobulin-like beta-sandwich	Cu,Zn superoxide dismutase-like	Cu,Zn superoxide dismutase-like	Cu,Zn superoxide dismutase, SOD	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Cu, Zn superoxide dismutase-like	8055259	3002059	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Sod_Cu	e1f1aA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Cu,Zn superoxide dismutase-like	F: Sod_Cu	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.200	Mainly Beta	Sandwich	Immunoglobulin-like	Superoxide dismutase, copper/zinc binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00080	Copper/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

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	COPPER-ZINC SUPEROXIDE DISMUTASE	superoxide dismutase activity oxidoreductase activity, acting on superoxide radicals as acceptor oxidoreductase activity antioxidant activity catalytic activity oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity, acting on a sulfur group of donors, oxygen as acceptor cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding	cellular respiration regulation of biological process regulation of cellular process energy derivation by oxidation of organic compounds negative regulation of cellular respiration negative regulation of metabolic process biological regulation negative regulation of biological process regulation of generation of precursor metabolites and energy generation of precursor metabolites and energy regulation of cellular respiration negative regulation of cellular process metabolic process cellular process cellular respiration regulation of biological process regulation of cellular process energy derivation by oxidation of organic compounds negative regulation of cellular respiration negative regulation of metabolic process biological regulation negative regulation of biological process regulation of generation of precursor metabolites and energy generation of precursor metabolites and energy regulation of cellular respiration negative regulation of cellular process metabolic process cellular process regulation of metabolic process regulation of protein stability regulation of biological quality protein stabilization biosynthetic process protein maturation by copper ion transfer primary metabolic process protein metabolic process macromolecule metabolic process gene expression macromolecule biosynthetic process protein maturation inorganic ion homeostasis homeostatic process intracellular copper ion homeostasis copper ion homeostasis cellular homeostasis chemical homeostasis intracellular monoatomic cation homeostasis monoatomic ion homeostasis intracellular chemical homeostasis monoatomic cation homeostasis intracellular monoatomic ion homeostasis cellular response to stimulus response to stimulus cellular response to oxidative stress detoxification reactive oxygen species metabolic process cellular response to chemical stress response to superoxide cellular oxidant detoxification cellular response to oxygen radical cellular response to reactive oxygen species cellular response to stress response to stress cellular detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to reactive oxygen species response to toxic substance removal of superoxide radicals superoxide metabolic process response to oxidative stress cellular response to chemical stimulus response to chemical cellular response to superoxide cellular response to toxic substance response to oxygen radical fungal-type cell wall organization cellular component organization fungal-type cell wall organization or biogenesis cell wall organization or biogenesis cell wall organization cellular component organization or biogenesis external encapsulating structure organization positive regulation of DNA-templated transcription positive regulation of biological process RNA metabolic process positive regulation of macromolecule biosynthetic process regulation of primary metabolic process nucleobase-containing compound metabolic process RNA biosynthetic process nucleic acid biosynthetic process positive regulation of metabolic process DNA-templated transcription regulation of RNA metabolic process transcription by RNA polymerase II positive regulation of biosynthetic process positive regulation of macromolecule metabolic process regulation of nucleobase-containing compound metabolic process positive regulation of cellular process regulation of RNA biosynthetic process regulation of biosynthetic process regulation of transcription by RNA polymerase II positive regulation of nucleobase-containing compound metabolic process regulation of macromolecule metabolic process positive regulation of transcription by RNA polymerase II nucleobase-containing compound biosynthetic process nucleic acid metabolic process positive regulation of RNA metabolic process regulation of gene expression positive regulation of RNA biosynthetic process regulation of macromolecule biosynthetic process regulation of DNA-templated transcription intracellular zinc ion homeostasis	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle protein-containing complex catalytic complex oxidoreductase complex superoxide dismutase complex cytosol mitochondrial intermembrane space membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle protein-containing complex catalytic complex oxidoreductase complex superoxide dismutase complex cytosol mitochondrial intermembrane space membrane-enclosed lumen intracellular organelle lumen organelle envelope lumen organelle envelope organelle lumen mitochondrial envelope nucleus

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR024134	Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone	Family
A	IPR001424	Superoxide dismutase, copper/zinc binding domain	Domain
A	IPR036423	Superoxide dismutase-like, copper/zinc binding domain superfamily	Homologous Superfamily
A	IPR018152	Superoxide dismutase, copper/zinc, binding site	Binding Site

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.