1GP1

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004601	molecular_function	peroxidase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005739	cellular_component	mitochondrion
A	0005829	cellular_component	cytosol
A	0006629	biological_process	lipid metabolic process
A	0006749	biological_process	glutathione metabolic process
A	0006979	biological_process	response to oxidative stress
A	0009650	biological_process	UV protection
A	0010269	biological_process	response to selenium ion
A	0016491	molecular_function	oxidoreductase activity
A	0017124	molecular_function	SH3 domain binding
A	0019369	biological_process	arachidonate metabolic process
A	0019372	biological_process	lipoxygenase pathway
A	0033599	biological_process	regulation of mammary gland epithelial cell proliferation
A	0034599	biological_process	cellular response to oxidative stress
A	0040029	biological_process	epigenetic regulation of gene expression
A	0042542	biological_process	response to hydrogen peroxide
A	0042744	biological_process	hydrogen peroxide catabolic process
A	0045454	biological_process	cell redox homeostasis
A	0047066	molecular_function	phospholipid-hydroperoxide glutathione peroxidase activity
A	0060047	biological_process	heart contraction
A	0061136	biological_process	regulation of proteasomal protein catabolic process
A	0090201	biological_process	negative regulation of release of cytochrome c from mitochondria
A	0097413	cellular_component	Lewy body
A	0098869	biological_process	cellular oxidant detoxification
A	1902042	biological_process	negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
A	1902905	biological_process	positive regulation of supramolecular fiber organization
A	1990782	molecular_function	protein tyrosine kinase binding
B	0004601	molecular_function	peroxidase activity
B	0004602	molecular_function	glutathione peroxidase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005739	cellular_component	mitochondrion
B	0005829	cellular_component	cytosol
B	0006629	biological_process	lipid metabolic process
B	0006749	biological_process	glutathione metabolic process
B	0006979	biological_process	response to oxidative stress
B	0009650	biological_process	UV protection
B	0010269	biological_process	response to selenium ion
B	0016491	molecular_function	oxidoreductase activity
B	0017124	molecular_function	SH3 domain binding
B	0019369	biological_process	arachidonate metabolic process
B	0019372	biological_process	lipoxygenase pathway
B	0033599	biological_process	regulation of mammary gland epithelial cell proliferation
B	0034599	biological_process	cellular response to oxidative stress
B	0040029	biological_process	epigenetic regulation of gene expression
B	0042542	biological_process	response to hydrogen peroxide
B	0042744	biological_process	hydrogen peroxide catabolic process
B	0045454	biological_process	cell redox homeostasis
B	0047066	molecular_function	phospholipid-hydroperoxide glutathione peroxidase activity
B	0060047	biological_process	heart contraction
B	0061136	biological_process	regulation of proteasomal protein catabolic process
B	0090201	biological_process	negative regulation of release of cytochrome c from mitochondria
B	0097413	cellular_component	Lewy body
B	0098869	biological_process	cellular oxidant detoxification
B	1902042	biological_process	negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
B	1902905	biological_process	positive regulation of supramolecular fiber organization
B	1990782	molecular_function	protein tyrosine kinase binding

Functional Information from PROSITE/UniProt

site_id	PS00460
Number of Residues	16
Details	GLUTATHIONE_PEROXID_1 Glutathione peroxidases active site. GKvLLIeNVaSlUGtT

Chain	Residue	Details
A	GLY33-THR48

---

site_id	PS00763
Number of Residues	8
Details	GLUTATHIONE_PEROXID_2 Glutathione peroxidases signature 2. LGFPCNQF

Chain	Residue	Details
A	LEU70-PHE77

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"O70325","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	Site: {"description":"Not glycated","evidences":[{"source":"PubMed","id":"7873592","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Subject to oxidation and hydroselenide loss to dehydroalanine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Non-standard residue: {"description":"Selenocysteine","evidences":[{"source":"UniProtKB","id":"P11352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P04041","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P11352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P11352","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (Glc) (glycation) lysine; in vitro","evidences":[{"source":"PubMed","id":"7873592","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 6852035

Chain	Residue	Details
A	GLN80
A	SEC45
A	TRP158

---

site_id	CSA2
Number of Residues	2
Details	a catalytic site defined by CSA, PubMed 6852035

Chain	Residue	Details
B	GLN80
B	TRP158

---

site_id	MCSA1
Number of Residues	3
Details	M-CSA 851

Chain	Residue	Details
A	SE745	covalent catalysis, proton shuttle (general acid/base)
A	LYS84	electrostatic stabiliser
A	LYS162	proton shuttle (general acid/base)

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 851

Chain	Residue	Details
B	SE745	covalent catalysis, proton shuttle (general acid/base)
B	LYS84	electrostatic stabiliser
B	LYS162	proton shuttle (general acid/base)

---