Structure of PDB 6nh6 Chain A

Receptor sequence

>6nh6A (length=404) Species: 9606 (Homo sapiens)

FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRKLAPEQLLSQ
ARDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATAS
FMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQ
PDPW

3D structure

• PDB: 6nh6 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
• Chain: A
• Resolution: 2.189 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C184 R187 W356 E361
• 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	W178 A181 R183 C184 F353 W356 E361 W447 F473 Y475	W102 A105 R107 C108 F277 W280 E285 W371 F397 Y399
BS02	H4B	A	S102 R365 W447	S35 R289 W371
BS03	KL7	A	F105 P334 V336 F353 W356 E361	F38 P258 V260 F277 W280 E285
BS04	ZN	A	C94 C99	C27 C32
BS05	H4B	A	W445 F460	W369 F384

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:6nh6, PDBe:6nh6, PDBj:6nh6
• PDBsum: 6nh6
• PubMed: 30802056
• UniProt: P29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)