Structure of PDB 3fjo Chain A

Receptor sequence
>3fjoA (length=603) Species: 9606,559292 [Search protein sequence]
NRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADV
ENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLR
YNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDY
MAWKDSILEVLKDELGVEATGEESSIRQYELVVHTDIDAAKVYMGEMGRL
KSYENQKPPFDAKNPFLAAVTTNRKLNQGTERHLMHLELDISDSKIRYES
GDHVAVYPANDSALVNQLGKILGADLDVVMSLNNLDEESNKKHPFPCPTS
YRTALTYYLDITNPPRTNVLYELAQYASEPSEQELLRKMASSSGEGKELY
LSWVVEARRHILAILQDCPSLRPPIDHLCELLPRLQARYYSIASSSKVHP
NSVHICAVVVEYETKAGRINKGVATNWLRAKEPARALVPMFVRKSQFRLP
FKATTPVIMVGPGTGVAPFIGFIQERAWLRQQGKEVGETLLYYGCRRSDE
DYLYREELAQFHRDGALTQLNVAFSRHKVYVQHLLKQDREHLWKLIEGGA
HIYVCGDARNMARDVQNTFYDIVAELGAMEHAQAVDYIKKLMTKGRYSLD
VWS
3D structure
PDB3fjo Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y436 S437 C609 D654 W656
Catalytic site (residue number reindexed from 1) Y390 S391 C555 D600 W602
Enzyme Commision number 1.6.2.4: NADPH--hemoprotein reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FMN A S67 Q68 T69 T71 A72 S116 T117 Y118 G153 N154 Y157 F160 S21 Q22 T23 T25 A26 S70 T71 Y72 G107 N108 Y111 F114
BS02 FAD A H299 R404 R434 Y435 Y436 S437 C452 Y458 G468 V469 A470 T471 W656 H253 R358 R388 Y389 Y390 S391 C406 Y412 G422 V423 A424 T425 W602
Gene Ontology
Molecular Function
GO:0003958 NADPH-hemoprotein reductase activity
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

View graph for
Molecular Function
External links
PDB RCSB:3fjo, PDBe:3fjo, PDBj:3fjo
PDBsum3fjo
PubMed19483672
UniProtP16435|NCPR_HUMAN NADPH--cytochrome P450 reductase (Gene Name=POR);
P16603|NCPR_YEAST NADPH--cytochrome P450 reductase (Gene Name=NCP1)

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