Structure of PDB 1f26 Chain A

Receptor sequence
>1f26A (length=399) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
APSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFV
ATSEKLSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPT
FTPEAVKNLQPYIQRTVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIY
TLLGVPFNDLEYLTQQNAIRTNGSSTAREASAANQELLDYLAILVEQRLV
EPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVAGNAVMVNMIALGVAT
LAQHPDQLAQLKANPSLAPQFVEELCRYHTASALAIKRTAKEDVMIGDKL
VRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIA
EHLAKAELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF
3D structure
PDB1f26 Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T175 A239 A242 V243 M244 S286 C352 I353 A354 E361 D393
Catalytic site (residue number reindexed from 1) T171 A235 A238 V239 M240 S282 C348 I349 A350 E357 D389
Enzyme Commision number 1.7.1.14: nitric oxide reductase [NAD(P)(+), nitrous oxide-forming].
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 HEM A F86 V87 R98 I153 L236 A239 G240 V243 M244 G344 F345 G346 F347 H350 C352 I353 A354 A358 F82 V83 R94 I149 L232 A235 G236 V239 M240 G340 F341 G342 F343 H346 C348 I349 A350 A354
BS02 NO A A239 G240 A235 G236
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0102199 nitric oxide reductase (NAD(P)H) activity

View graph for
Molecular Function
External links
PDB RCSB:1f26, PDBe:1f26, PDBj:1f26
PDBsum1f26
PubMed11132616
UniProtP23295|NOR_FUSOX NADP nitrous oxide-forming nitric oxide reductase (Gene Name=CYP55A1)

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