1GP1

THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1gp1a_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Glutathione peroxidase	bovine (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d1gp1b_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Glutathione peroxidase	bovine (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Glutathione peroxidase-like	8057880	4000042	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioredoxin-like	8057881	3000031	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Thioredoxin-like	8057881	3000031	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	GSHPx	e1gp1A1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GSHPx	ECOD (1.6)
B	GSHPx	e1gp1B1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: GSHPx	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00255	Glutathione peroxidase (GSHPx)	Glutathione peroxidase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GLUTATHIONE PEROXIDASE	phospholipid-hydroperoxide glutathione peroxidase activity peroxidase activity oxidoreductase activity antioxidant activity oxidoreductase activity, acting on peroxide as acceptor catalytic activity glutathione peroxidase activity	catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process icosanoid metabolic process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process small molecule metabolic process lipoxygenase pathway catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process icosanoid metabolic process fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process primary metabolic process organic acid metabolic process small molecule metabolic process lipoxygenase pathway monocarboxylic acid metabolic process lipid metabolic process response to stimulus response to chemical response to selenium ion long-chain fatty acid metabolic process unsaturated fatty acid metabolic process arachidonate metabolic process olefinic compound metabolic process regulation of biological process regulation of cellular component organization regulation of cellular process positive regulation of cellular component organization biological regulation positive regulation of biological process positive regulation of supramolecular fiber organization cellular component organization regulation of supramolecular fiber organization cellular component organization or biogenesis supramolecular fiber organization positive regulation of cellular process response to hydrogen peroxide response to oxidative stress response to stress response to oxygen-containing compound response to reactive oxygen species glutathione metabolic process modified amino acid metabolic process sulfur compound metabolic process amide metabolic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR029759	Glutathione peroxidase active site	Active Site
A, B	IPR029760	Glutathione peroxidase conserved site	Conserved Site
A, B	IPR000889	Glutathione peroxidase	Family
A, B	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	glutathione peroxidase M-CSA #851	Glutathione peroxidase (GSHPx) is an enzyme that catalyses the reduction of hydroxyperoxides by glutathione. Its main function is to protect against the damaging effect of endogenously formed hydroxyperoxides.	Defined by 3 residues: SEC:A-45GLN:A-80TRP:A-158 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.11.1.9 (PDB Primary Data) Search M-CSA Motif + EC 1.11.1.9 EC: 1.11.1.12 (UniProt) Search M-CSA Motif + EC 1.11.1.12

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.