Structure of PDB 5vva Chain B

Receptor sequence

>5vvaB (length=404) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW

3D structure

• PDB: 5vva Hydrophilic, Potent, and Selective 7-Substituted 2-Aminoquinolines as Improved Human Neuronal Nitric Oxide Synthase Inhibitors.
• Chain: B
• Resolution: 2.55 Å

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	H4B	B	F462 H463 E465	F384 H385 E387
BS02	ZN	B	C96 C101	C28 C33
BS03	HEM	B	W180 C186 V187 S228 M341 F355 W358 E363 F475 Y477	W102 C108 V109 S150 M263 F277 W280 E285 F397 Y399
BS04	H4B	B	S104 R367 A448 W449	S36 R289 A370 W371
BS05	9OJ	B	L107 V338 F355 W358 E363 W449 Y477	L39 V260 F277 W280 E285 W371 Y399	BindingDB: Ki=468nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:5vva, PDBe:5vva, PDBj:5vva
• PDBsum: 5vva
• PubMed: 28776992
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)