Structure of PDB 3n6b Chain B

Receptor sequence
>3n6bB (length=402) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPPAEQLLSQAR
DFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPSRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFM
KHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPD
PW
3D structure
PDB3n6b Role of zinc in isoform-selective inhibitor binding to neuronal nitric oxide synthase .
ChainB
Resolution3.1 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) 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 B W447 F462 H463 Q464 W367 F382 H383 Q384
BS02 ZN B C96 C101 C28 C33
BS03 HEM B W180 R185 C186 G188 M341 F355 W358 M360 E363 W449 W100 R105 C106 G108 M261 F275 W278 M280 E283 W369
BS04 H4B B R367 A448 W449 R287 A368 W369
BS05 XFJ B P336 W358 E363 P256 W278 E283 BindingDB: Ki=25nM
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:3n6b, PDBe:3n6b, PDBj:3n6b
PDBsum3n6b
PubMed21138269
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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