Structure of PDB 5uod Chain B

Receptor sequence

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

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW

3D structure

• PDB: 5uod Nitrile in the Hole: Discovery of a Small Auxiliary Pocket in Neuronal Nitric Oxide Synthase Leading to the Development of Potent and Selective 2-Aminoquinoline Inhibitors.
• Chain: B
• Resolution: 2.01 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	W447 F462 Q464	W369 F384 Q386
BS02	ZN	B	C96 C101	C28 C33
BS03	HEM	B	W180 R185 C186 S228 F355 W358 E363 W449 F475 Y477	W102 R107 C108 S150 F277 W280 E285 W371 F397 Y399
BS04	H4B	B	S104 R367 A448 W449	S36 R289 A370 W371
BS05	8EY	B	P336 V338 N340 M341 W358 E363 Y477	P258 V260 N262 M263 W280 E285 Y399

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:5uod, PDBe:5uod, PDBj:5uod
• PDBsum: 5uod
• PubMed: 28422508
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)