Structure of PDB 1cmj Chain A

Receptor sequence

>1cmjA (length=399) Species: 5507 (Fusarium oxysporum)

APSFPFSRASGPEPPAEFAKLRATNPVSQVKLFDGSLAWLVTKHKDVCFV
ATSEKLSKVRTRQGFPELSASGKQAAKAKPTFVDMDPPEHMHQRSMVEPT
FTPEAVKNLQPYIQRTVDDLLEQMKQKGCANGPVDLVKEFALPVPSYIIY
TLLGVPFNDLEYLTQQNAIRTNGSSTAREASAANQELLDYLAILVEQRLV
EPKDDIISKLCTEQVKPGNIDKSDAVQIAFLLLVAGNATMVNMIALGVAT
LAQHPDQLAQLKANPSLAPQFVEELCRYHTATALAIKRTAKEDVMIGDKL
VRANEGIIASNQSANRDEEVFENPDEFNMNRKWPPQDPLGFGFGDHRCIA
EHLAKAELTTVFSTLYQKFPDLKVAVPLGKINYTPLNRDVGIVDLPVIF

3D structure

• PDB: 1cmj Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): T175 A239 A242 T243 M244 T286 C352 I353 A354 E361 D393
• Catalytic site (residue number reindexed from 1): T171 A235 A238 T239 M240 T282 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 H94 R98 L236 A239 G240 T243 M244 G344 F345 G346 F347 H350 C352 I353 A354	F82 V83 H90 R94 L232 A235 G236 T239 M240 G340 F341 G342 F343 H346 C348 I349 A350

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

External links

• PDB: RCSB:1cmj, PDBe:1cmj, PDBj:1cmj
• PDBsum: 1cmj
• PubMed: 10671516
• UniProt: P23295|NOR_FUSOX NADP nitrous oxide-forming nitric oxide reductase (Gene Name=CYP55A1)