3C1S

Crystal structure of GRX1 in glutathionylated form

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004364	molecular_function	glutathione transferase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0015038	molecular_function	glutathione disulfide oxidoreductase activity
A	0016491	molecular_function	oxidoreductase activity
A	0016740	molecular_function	transferase activity
A	0034599	biological_process	cellular response to oxidative stress
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE GSH A 2001

Chain	Residue
A	LYS24
A	ASP89
A	HOH2013
A	HOH2019
A	HOH2036
A	HOH2037
A	HOH2039
A	HOH2041
A	TYR26
A	CYS27
A	TYR29
A	GLN63
A	THR74
A	PRO76
A	GLY87
A	ASN88

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Functional Information from PROSITE/UniProt

site_id	PS00195
Number of Residues	17
Details	GLUTAREDOXIN_1 Glutaredoxin active site. VAsktyCPYChaAlntL

Chain	Residue	Details
A	VAL21-LEU37

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17327665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18473363","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"S-glutathionyl cysteine; alternate","evidences":[{"source":"PubMed","id":"17327665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18473363","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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