Structure of PDB 6nh7 Chain B

Receptor sequence
>6nh7B (length=402) Species: 9606 (Homo sapiens) [Search protein sequence]
KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQAR
DFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFM
KHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPD
PW
3D structure
PDB6nh7 Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having a 2-Aminopyridine Scaffold.
ChainB
Resolution1.9 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 KMM B W74 F460 W8 F382
BS02 ZN B C94 C99 C28 C33
BS03 HEM B W178 C184 F353 W356 E361 F473 Y475 W100 C106 F275 W278 E283 F395 Y397
BS04 KMM B F105 Q247 P334 V336 F353 W356 E361 Y475 F39 Q169 P256 V258 F275 W278 E283 Y397
BS05 KMM B H371 A446 W447 H293 A368 W369
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:6nh7, PDBe:6nh7, PDBj:6nh7
PDBsum6nh7
PubMed30802056
UniProtP29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)

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