Structure of PDB 6nh7 Chain A

Receptor sequence

>6nh7A (length=401) Species: 9606 (Homo sapiens)

FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQARD
FINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWR
NAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAIT
VFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW
TPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGLR
WYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDV
AVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMK
HLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDP
W

3D structure

• PDB: 6nh7 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C184 R187 W356 E361
• Catalytic site (residue number reindexed from 1): C105 R108 W277 E282
• 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 C184 F353 W356 E361 W447 F473 Y475	W99 C105 F274 W277 E282 W368 F394 Y396
BS02	KMM	A	F105 Q247 V336 F353 W356 E361 W447	F38 Q168 V257 F274 W277 E282 W368
BS03	KMM	A	H371 W447	H292 W368
BS04	ZN	A	C94 C99	C27 C32
BS05	KMM	A	W74 W445 F460	W7 W366 F381

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:6nh7, PDBe:6nh7, PDBj:6nh7
• PDBsum: 6nh7
• PubMed: 30802056
• UniProt: P29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)