9H9C

Crystal structure of thioredoxin reductase from Cryptosporidium parvum in the "activated in" conformation

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
AAA	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
AAA	0016491	molecular_function	oxidoreductase activity
AAA	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
AAA	0045454	biological_process	cell redox homeostasis
AAA	0050660	molecular_function	flavin adenine dinucleotide binding
BBB	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
BBB	0016491	molecular_function	oxidoreductase activity
BBB	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
BBB	0045454	biological_process	cell redox homeostasis
BBB	0050660	molecular_function	flavin adenine dinucleotide binding
CCC	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
CCC	0016491	molecular_function	oxidoreductase activity
CCC	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
CCC	0045454	biological_process	cell redox homeostasis
CCC	0050660	molecular_function	flavin adenine dinucleotide binding
DDD	0004791	molecular_function	thioredoxin-disulfide reductase (NADPH) activity
DDD	0016491	molecular_function	oxidoreductase activity
DDD	0016668	molecular_function	oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
DDD	0045454	biological_process	cell redox homeostasis
DDD	0050660	molecular_function	flavin adenine dinucleotide binding

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
AAA	GLY71-PRO81

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