Structure of PDB 5vvd Chain D

Receptor sequence
>5vvdD (length=402) Species: 9606 (Homo sapiens) [Search protein sequence]
KFPRVKNWEVGSITYDTLSAQAQQDGPCTPRRCLGSLVFPAPEQLLSQAR
DFINQYYSSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCRSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRCPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEPPELFLLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFPAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFM
KHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPD
PW
3D structure
PDB5vvd Hydrophilic, Potent, and Selective 7-Substituted 2-Aminoquinolines as Improved Human Neuronal Nitric Oxide Synthase Inhibitors.
ChainD
Resolution2.25 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 H4B D W445 F460 E463 W367 F382 E385
BS02 ZN D C94 C99 C28 C33
BS03 HEM D W178 A181 R183 C184 F353 S354 W356 E361 W447 F473 Y475 W100 A103 R105 C106 F275 S276 W278 E283 W369 F395 Y397
BS04 H4B D R365 A446 W447 R287 A368 W369
BS05 9OG D F105 V336 F353 E361 F39 V258 F275 E283 BindingDB: Ki=5790nM
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:5vvd, PDBe:5vvd, PDBj:5vvd
PDBsum5vvd
PubMed28776992
UniProtP29474|NOS3_HUMAN Nitric oxide synthase 3 (Gene Name=NOS3)

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