Structure of PDB 3n69 Chain A

Receptor sequence
>3n69A (length=404) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLMLPPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRDLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW
3D structure
PDB3n69 Role of zinc in isoform-selective inhibitor binding to neuronal nitric oxide synthase .
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C108 R111 W280 E285
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 A W180 C186 V187 F355 S356 W358 E363 F475 W102 C108 V109 F277 S278 W280 E285 F397
BS02 H4B A S104 R367 A448 W449 S38 R289 A370 W371
BS03 XFJ A M106 Q249 P336 V338 F355 E363 Y477 M40 Q171 P258 V260 F277 E285 Y399 BindingDB: Ki=25nM
BS04 ZN A C96 C101 C30 C35
BS05 H4B A W447 F462 W369 F384
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:3n69, PDBe:3n69, PDBj:3n69
PDBsum3n69
PubMed21138269
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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