Structure of PDB 1p6m Chain A

Receptor sequence
>1p6mA (length=404) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW
3D structure
PDB1p6m Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase.
ChainA
Resolution2.27 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 R185 C186 F355 S356 W358 E363 W449 F475 Y477 W102 R107 C108 F277 S278 W280 E285 W371 F397 Y399
BS02 H4B A S104 V106 R367 A448 W449 S38 V40 R289 A370 W371
BS03 DP3 A S356 W358 E363 S278 W280 E285 MOAD: Ki=80uM
BS04 ZN A C96 C101 C30 C35
BS05 H4B A W447 F462 W369 F384
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1p6m, PDBe:1p6m, PDBj:1p6m
PDBsum1p6m
PubMed14718923
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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