Structure of PDB 1f26 Chain A Binding Site BS02
Receptor Information
>1f26 Chain A (length=399) Species:
5507
(Fusarium oxysporum) [
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APSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFV
ATSEKLSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPT
FTPEAVKNLQPYIQRTVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIY
TLLGVPFNDLEYLTQQNAIRTNGSSTAREASAANQELLDYLAILVEQRLV
EPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVAGNAVMVNMIALGVAT
LAQHPDQLAQLKANPSLAPQFVEELCRYHTASALAIKRTAKEDVMIGDKL
VRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIA
EHLAKAELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF
Ligand information
Ligand ID
NO
InChI
InChI=1S/HNO/c1-2/h1H
InChIKey
ODUCDPQEXGNKDN-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.385
OpenEye OEToolkits 2.0.7
[N]=O
Formula
N O
Name
NITRIC OXIDE;
Nitrogen monoxide
ChEMBL
CHEMBL1234765
DrugBank
ZINC
PDB chain
1f26 Chain A Residue 502 [
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Receptor-Ligand Complex Structure
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PDB
1f26
Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function.
Resolution
1.4 Å
Binding residue
(original residue number in PDB)
A239 G240
Binding residue
(residue number reindexed from 1)
A235 G236
Annotation score
1
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].
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
PDBsum
1f26
PubMed
11132616
UniProt
P23295
|NOR_FUSOX NADP nitrous oxide-forming nitric oxide reductase (Gene Name=CYP55A1)
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