5VDN

1.55 Angstrom Resolution Crystal Structure of Glutathione Reductase from Yersinia pestis in Complex with FAD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004362	molecular_function	glutathione-disulfide reductase (NADPH) activity
A	0005737	cellular_component	cytoplasm
A	0006749	biological_process	glutathione metabolic process
A	0016491	molecular_function	oxidoreductase activity
A	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
A	0045454	biological_process	cell redox homeostasis
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0050661	molecular_function	NADP binding
A	0098869	biological_process	cellular oxidant detoxification
B	0000166	molecular_function	nucleotide binding
B	0004362	molecular_function	glutathione-disulfide reductase (NADPH) activity
B	0005737	cellular_component	cytoplasm
B	0006749	biological_process	glutathione metabolic process
B	0016491	molecular_function	oxidoreductase activity
B	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
B	0045454	biological_process	cell redox homeostasis
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0050661	molecular_function	NADP binding
B	0098869	biological_process	cellular oxidant detoxification

Functional Information from PROSITE/UniProt

site_id	PS00076
Number of Residues	11
Details	PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP

Chain	Residue	Details
A	GLY49-PRO59

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