Structure of PDB 1foj Chain B

Receptor sequence
>1fojB (length=414) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW
3D structure
PDB1foj Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism
ChainB
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C118 R121 W290 E295
Enzyme Commision number 1.14.13.39: nitric-oxide synthase (NADPH).
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 ZN B C96 C101 C28 C33
BS02 HEM B W180 R185 C186 F355 S356 W358 E363 W449 F475 Y477 W112 R117 C118 F287 S288 W290 E295 W381 F407 Y409
BS03 7NI B G357 W358 Y359 E363 G289 W290 Y291 E295 BindingDB: IC50=35000nM
BS04 7I2 B W447 F462 H463 W379 F394 H395
BS05 7I2 B S104 A448 W449 S36 A380 W381
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1foj, PDBe:1foj, PDBj:1foj
PDBsum1foj
PubMed11695891
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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