Structure of PDB 5vv9 Chain B

Receptor sequence
>5vv9B (length=404) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW
3D structure
PDB5vv9 Hydrophilic, Potent, and Selective 7-Substituted 2-Aminoquinolines as Improved Human Neuronal Nitric Oxide Synthase Inhibitors.
ChainB
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) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C108 R111 W280 E285
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 HEM B W180 C186 V187 S228 F355 S356 W358 E363 F475 Y477 W102 C108 V109 S150 F277 S278 W280 E285 F397 Y399
BS02 H4B B R367 A448 W449 R289 A370 W371
BS03 9OG B L107 V338 F355 W358 E363 Y477 L39 V260 F277 W280 E285 Y399 MOAD: Ki=1.22uM
BindingDB: Ki=1220nM
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:5vv9, PDBe:5vv9, PDBj:5vv9
PDBsum5vv9
PubMed28776992
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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