Structure of PDB 6nh1 Chain C

Receptor sequence
>6nh1C (length=402) Species: 9606 (Homo sapiens) [Search protein sequence]
KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQAR
DFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFM
KHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPD
PW
3D structure
PDB6nh1 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
ChainC
Resolution2.216 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C184 R187 W356 E361
Catalytic site (residue number reindexed from 1) C106 R109 W278 E283
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 V185 F353 S354 W356 E361 W447 F473 Y475 W100 C106 V107 F275 S276 W278 E283 W369 F395 Y397
BS02 H4B C S102 R365 S36 R287
BS03 KLY C W356 E361 W278 E283
BS04 ZN C C94 C99 C28 C33
BS05 H4B C F460 H461 F382 H383
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6nh1, PDBe:6nh1, PDBj:6nh1
PDBsum6nh1
PubMed30802056
UniProtP29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)

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