Structure of PDB 6nh6 Chain C

Receptor sequence

>6nh6C (length=401) Species: 9606 (Homo sapiens)

FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQARD
FINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWR
NAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAIT
VFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW
TPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGLR
WYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDV
AVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMK
HLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDP
W

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: C
• Resolution: 2.189 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	C	W178 C184 F353 W356 E361 W447 F473 Y475	W99 C105 F274 W277 E282 W368 F394 Y396
BS02	H4B	C	S102 R365 W447	S35 R286 W368
BS03	KL7	C	P334 V336 W356 E361 Y475	P255 V257 W277 E282 Y396
BS04	ZN	C	C94 C99	C27 C32

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)