1amo Summary

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THREE-DIMENSIONAL STRUCTURE OF NADPH-CYTOCHROME P450 REDUCTASE: PROTOTYPE FOR FMN-AND FAD-CONTAINING ENZYMES

The structure was published by Wang, M., Roberts, D.L., Paschke, R., Shea, T.M., Masters, B.S., and Kim, J.J., in 1997 in a paper entitled "Three-dimensional structure of NADPH-cytochrome P450 reductase: prototype for FMN- and FAD-containing enzymes." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.6 Å and deposited in 1997.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of NADPH-CYTOCHROME P450 REDUCTASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A NADPH-CYTOCHROME P450 REDUCTASE P00388 (64-678) (NCPR_RAT)search Rattus norvegicussearch 91% 615 97%
B NADPH-CYTOCHROME P450 REDUCTASE P00388 (64-678) (NCPR_RAT)search Rattus norvegicussearch 91% 615 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00388 (64 - 678) NADPH-CYTOCHROME P450 REDUCTASE Rattus norvegicus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P00388) NADPH-cytochrome p450 reductase FAD-binding domain-likesearch, Cytochrome p450 reductase N-terminal domain-likesearch, NADPH-cytochrome p450 reductase-likesearch Rossmann foldsearch, Translation factorssearch, NADPH-cytochrome p450 Reductase; Chain A, domain 3search, Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) modulesearch PF00175: Oxidoreductase NAD-binding domainsearch, PF00258: Flavodoxinsearch, PF00667: FAD binding domainsearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A, B (P00388) positive regulation of chondrocyte differentiationsearch internal peptidyl-lysine acetylationsearch negative regulation of cysteine-type endopeptidase activity involved in apoptotic processsearch positive regulation of steroid hormone biosynthetic processsearch oxidation-reduction processsearch fatty acid oxidationsearch negative regulation of apoptotic processsearch cellular organofluorine metabolic processsearch response to drugsearch nitric oxide catabolic processsearch cellular response to peptide hormone stimulussearch nitrate catabolic processsearch negative regulation of lipase activitysearch cellular response to follicle-stimulating hormone stimulussearch carnitine metabolic processsearch positive regulation of monooxygenase activitysearch response to nutrientsearch regulation of cholesterol metabolic processsearch demethylationsearch flavonoid metabolic processsearch positive regulation of cholesterol biosynthetic processsearch positive regulation of smoothened signaling pathwaysearch cellular response to gonadotropin stimulussearch regulation of growth plate cartilage chondrocyte proliferationsearch membranesearch intracellular membrane-bounded organellesearch endoplasmic reticulum membranesearch endoplasmic reticulumsearch mitochondrionsearch cytosolsearch enzyme bindingsearch oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygensearch oxidoreductase activitysearch FMN bindingsearch cytochrome-b5 reductase activity, acting on NAD(P)Hsearch hydrolase activitysearch iron ion bindingsearch NADP bindingsearch nitric oxide dioxygenase activitysearch NADPH-hemoprotein reductase activitysearch flavin adenine dinucleotide bindingsearch electron carrier activitysearch iron-cytochrome-c reductase activitysearch

Chain InterPro annotation
A, B Flavodoxinsearch Oxidoreductase FAD/NAD(P)-bindingsearch Flavoprotein pyridine nucleotide cytochrome reductasesearch FAD-binding, type 1search Flavodoxin/nitric oxide synthasesearch Ferredoxin reductase-type FAD-binding domainsearch Riboflavin synthase-like beta-barrelsearch NADPH-cytochrome p450 reductase, FAD-binding, alpha-helical domain-3search