1QMV

thioredoxin peroxidase B from red blood cells

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
Pharos: Disease Associations
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d1qmvb_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1qmvc_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1qmvd_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
G	d1qmvg_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
H	d1qmvh_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
I	d1qmvi_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d1qmva_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d1qmve_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d1qmvf_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
J	d1qmvj_	Alpha and beta proteins (a/b)	Thioredoxin fold	Thioredoxin-like	Glutathione peroxidase-like	Thioredoxin peroxidase 2 (thioredoxin peroxidase B, 2-cys peroxiredoxin)	(Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
I	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
A	SCOP2 Family	Glutathione peroxidase-like	8057891	4000042	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Thioredoxin-like	8057892	3000031	SCOP2 (2022-06-29)
E	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Thioredoxin-like	8057892	3000031	SCOP2B (2022-06-29)
J	SCOP2B Superfamily	Thioredoxin-like	8057892	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)
B	AhpC-TSA_1	e1qmvB1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
C	AhpC-TSA_1	e1qmvC1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
D	AhpC-TSA_1	e1qmvD1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
G	AhpC-TSA_1	e1qmvG1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
H	AhpC-TSA_1	e1qmvH1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
I	AhpC-TSA_1	e1qmvI1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
A	AhpC-TSA_1	e1qmvA1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
E	AhpC-TSA_1	e1qmvE1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
F	AhpC-TSA_1	e1qmvF1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)
J	AhpC-TSA_1	e1qmvJ1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: AhpC-TSA_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
C	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
D	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
G	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
H	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
I	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
A	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
E	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
F	3.40.30.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaredoxin	Glutaredoxin	CATH (4.3.0)
J	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, C, D, E A, B, C, D, E, F, G, H, I, J	PF00578	AhpC/TSA family (AhpC-TSA)	AhpC/TSA family	This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	PF10417	C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx_C)	C-terminal domain of 1-Cys peroxiredoxin	This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding al ...	This is the C-terminal domain of 1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin superfamily which protect cells against membrane oxidation through glutathione (GSH)-dependent reduction of phospholipid hydroperoxides to corresponding alcohols [1]. The C-terminal domain is crucial for providing the extra cysteine necessary for dimerisation of the whole molecule. Loss of the enzyme's peroxidase activity is associated with oxidation of the catalytic cysteine, upstream of this domain; and glutathionylation, presumably through its disruption of protein structure, facilitates access for GSH, resulting in spontaneous reduction of the mixed disulfide to the sulfhydryl and consequent activation of the enzyme [2]. The domain is associated with family AhpC-TSA, Pfam:PF00578, which carries the catalytic cysteine.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	PEROXIREDOXIN-2	antioxidant activity peroxidase activity oxidoreductase activity thioredoxin-dependent peroxiredoxin activity oxidoreductase activity, acting on peroxide as acceptor thioredoxin peroxidase activity catalytic activity peroxiredoxin activity	catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to tumor cell response to stimulus defense response response to stress defense response to tumor cell response to biotic stimulus cellular response to stimulus negative regulation of extrinsic apoptotic signaling pathway in absence of ligand catabolic process hydrogen peroxide metabolic process reactive oxygen species metabolic process metabolic process cellular process hydrogen peroxide catabolic process response to tumor cell response to stimulus defense response response to stress defense response to tumor cell response to biotic stimulus cellular response to stimulus negative regulation of extrinsic apoptotic signaling pathway in absence of ligand regulation of cellular process signal transduction in absence of ligand negative regulation of signaling signaling negative regulation of biological process regulation of signal transduction regulation of programmed cell death negative regulation of cell communication extrinsic apoptotic signaling pathway negative regulation of signal transduction in absence of ligand cell communication negative regulation of extrinsic apoptotic signaling pathway negative regulation of apoptotic signaling pathway negative regulation of cellular process extrinsic apoptotic signaling pathway in absence of ligand signal transduction regulation of signaling regulation of biological process cell surface receptor signaling pathway negative regulation of response to stimulus negative regulation of programmed cell death regulation of apoptotic process biological regulation cell death negative regulation of signal transduction regulation of extrinsic apoptotic signaling pathway apoptotic signaling pathway negative regulation of apoptotic process regulation of response to stimulus regulation of extrinsic apoptotic signaling pathway in absence of ligand regulation of cell communication apoptotic process programmed cell death regulation of apoptotic signaling pathway developmental process immune system development multicellular organismal process animal organ development gland development hematopoietic or lymphoid organ development multicellular organism development thymus development immune system process anatomical structure development system development cellular response to oxidative stress detoxification 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 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 cell activation leukocyte activation regulation of leukocyte differentiation regulation of leukocyte activation regulation of cell activation mononuclear cell differentiation regulation of cell differentiation lymphocyte differentiation regulation of cell development negative regulation of cell adhesion negative regulation of T cell differentiation T cell activation cell differentiation T cell differentiation regulation of immune system process negative regulation of hemopoiesis negative regulation of leukocyte differentiation negative regulation of T cell activation negative regulation of leukocyte cell-cell adhesion negative regulation of cell-cell adhesion regulation of leukocyte cell-cell adhesion negative regulation of lymphocyte differentiation negative regulation of multicellular organismal process negative regulation of leukocyte activation leukocyte differentiation cellular developmental process regulation of developmental process cell development lymphocyte activation negative regulation of lymphocyte activation leukocyte cell-cell adhesion regulation of T cell differentiation cell adhesion cell-cell adhesion regulation of multicellular organismal process regulation of cell-cell adhesion negative regulation of cell differentiation regulation of lymphocyte differentiation regulation of multicellular organismal development hemopoiesis negative regulation of developmental process regulation of cell adhesion regulation of T cell activation negative regulation of cell activation negative regulation of cell development negative regulation of immune system process regulation of hemopoiesis regulation of lymphocyte activation multicellular organismal-level homeostasis leukocyte homeostasis T cell homeostasis homeostatic process homeostasis of number of cells lymphocyte homeostasis regulation of hydrogen peroxide metabolic process regulation of metabolic process regulation of reactive oxygen species metabolic process cell population proliferation leukocyte proliferation mononuclear cell proliferation lymphocyte proliferation T cell proliferation positive regulation of cell communication positive regulation of signal transduction positive regulation of biological process intracellular signal transduction positive regulation of response to stimulus regulation of intracellular signal transduction intracellular signaling cassette positive regulation of cellular process positive regulation of MAPK cascade positive regulation of intracellular signal transduction regulation of MAPK cascade MAPK cascade positive regulation of signaling cell redox homeostasis cellular homeostasis regulation of lipopolysaccharide-mediated signaling pathway negative regulation of lipopolysaccharide-mediated signaling pathway regulation of response to biotic stimulus biological process involved in interspecies interaction between organisms negative regulation of response to biotic stimulus regulation of response to external stimulus response to lipid cellular response to lipopolysaccharide lipopolysaccharide-mediated signaling pathway cellular response to biotic stimulus response to bacterium response to external biotic stimulus response to other organism response to external stimulus cellular response to molecule of bacterial origin response to lipopolysaccharide negative regulation of response to external stimulus cellular response to lipid response to molecule of bacterial origin regulation of body fluid levels positive regulation of coagulation positive regulation of blood coagulation regulation of response to wounding regulation of coagulation regulation of response to stress coagulation positive regulation of hemostasis regulation of biological quality response to wounding regulation of hemostasis positive regulation of response to wounding wound healing regulation of blood coagulation hemostasis blood coagulation positive regulation of wound healing regulation of wound healing positive regulation of multicellular organismal process production of molecular mediator involved in inflammatory response respiratory burst involved in defense response immune effector process respiratory burst respiratory burst involved in inflammatory response inflammatory response	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR019479	Peroxiredoxin, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR024706	Peroxiredoxin, AhpC-type	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR050217	Thiol-specific antioxidant peroxiredoxin	Family
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR013766	Thioredoxin domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	IPR000866	Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	Pharos: P32119	osteosarcoma myeloid leukemia Down syndrome melanoma prostate cancer asbestosis carcinoma esophageal cancer Mammary Neoplasms, Experimental sarcomatoid carcinoma chronic monocytic leukemia keloid mammary neoplasms, animal oligodendroglioma pancreatic ductal adenocarcinoma osteosarcoma myeloid leukemia Down syndrome melanoma prostate cancer asbestosis carcinoma esophageal cancer Mammary Neoplasms, Experimental sarcomatoid carcinoma chronic monocytic leukemia keloid mammary neoplasms, animal oligodendroglioma pancreatic ductal adenocarcinoma acute myeloid leukemia cutaneous melanoma malignant mesothelioma pancreatic intraductal papillary-mucinous neoplasm astrocytic tumor tuberculosis hepatocellular carcinoma lung cancer neoplasm of esophagus ovarian cancer plasma cell myeloma psoriasis B-cell chronic lymphocytic leukemia undifferentiated carcinoma malignant ependymoma

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	CSD	Parent Component: CYS RESID: AA0262 PSI-MOD : L-cysteine sulfinic acid MOD:00267
A, B, C, D, E A, B, C, D, E, F, G, H, I, J	NCB	Parent Component: ALA RESID: AA0262

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.