Structure of PDB 6nh6 Chain D

Receptor sequence
>6nh6D (length=403) Species: 9606 (Homo sapiens) [Search protein sequence]
KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPRAPEQLLSQA
RDFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQA
WRNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSA
ITVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQH
GWTPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALG
LRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILE
DVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASF
MKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQP
DPW
3D structure
PDB6nh6 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
ChainD
Resolution2.189 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C184 R187 W356 E361
Catalytic site (residue number reindexed from 1) C107 R110 W279 E284
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 ZN D C94 C99 C28 C33
BS02 HEM D W178 R183 C184 S226 F353 W356 E361 W447 F473 Y475 W101 R106 C107 S149 F276 W279 E284 W370 F396 Y398
BS03 H4B D R365 A446 W447 R288 A369 W370
BS04 KL7 D P334 V336 F353 E361 W447 P257 V259 F276 E284 W370
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:6nh6, PDBe:6nh6, PDBj:6nh6
PDBsum6nh6
PubMed30802056
UniProtP29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)

[Back to BioLiP]