Structure of PDB 1d1y Chain B

Receptor sequence
>1d1yB (length=414) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW
3D structure
PDB1d1y Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.
ChainB
Resolution2.2 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) C118 R121 W290 E295
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 ZN B C96 C101 C28 C33
BS02 HEM B W180 R185 C186 V187 F355 W358 E363 W449 F475 Y477 W112 R117 C118 V119 F287 W290 E295 W381 F407 Y409
BS03 3BT B Q249 P336 V338 W358 E363 Q181 P268 V270 W290 E295
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:1d1y, PDBe:1d1y, PDBj:1d1y
PDBsum1d1y
PubMed11331290
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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