Structure of PDB 6nh4 Chain C

Receptor sequence

>6nh4C (length=401) Species: 9606 (Homo sapiens)

FPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQARD
FINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWR
NAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAIT
VFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW
TPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGLR
WYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILEDV
AVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMK
HLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDP
W

3D structure

• PDB: 6nh4 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
• Chain: C
• Resolution: 2.27 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 R183 C184 M339 F353 W356 E361 R365 F473 Y475	W99 R104 C105 M260 F274 W277 E282 R286 F394 Y396
BS02	H4B	C	S102 W447	S35 W368
BS03	KLA	C	F105 P334 F353 W356 E361 R365 Y475	F38 P255 F274 W277 E282 R286 Y396
BS04	ZN	C	C94 C99	C27 C32
BS05	KLA	C	W74 F460	W7 F381

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:6nh4, PDBe:6nh4, PDBj:6nh4
• PDBsum: 6nh4
• PubMed: 30802056
• UniProt: P29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)