Structure of PDB 4uha Chain A

Receptor sequence

>4uhaA (length=404) Species: 9913 (Bos taurus)

GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW

3D structure

• PDB: 4uha 2-Aminopyridines with a Truncated Side Chain To Improve Human Neuronal Nitric Oxide Synthase Inhibitory Potency and Selectivity.
• Chain: A
• Resolution: 2.2 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	HEM	A	W180 R185 C186 S228 F355 S356 W358 E363 W449 F475 Y477	W102 R107 C108 S150 F277 S278 W280 E285 W371 F397 Y399
BS02	H4B	A	S104 V106 R367 A448 W449	S38 V40 R289 A370 W371
BS03	Q1T	A	P336 V338 F355 W358 E363 R367	P258 V260 F277 W280 E285 R289	MOAD: Ki=24950nM BindingDB: Ki=24950nM
BS04	ZN	A	C96 C101	C30 C35
BS05	H4B	A	W447 F462 H463 E465	W369 F384 H385 E387

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:4uha, PDBe:4uha, PDBj:4uha
• PDBsum: 4uha
• PubMed: 26120733
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)