Structure of PDB 1d1w Chain B

Receptor sequence
>1d1wB (length=414) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW
3D structure
PDB1d1w Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
ChainB
Resolution2.0 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 H4B B W447 F462 E465 W379 F394 E397
BS03 HEM B W180 C186 V187 S228 M341 F355 W358 E363 F475 Y477 W112 C118 V119 S160 M273 F287 W290 E295 F407 Y409
BS04 H4B B S104 R367 A448 W449 S36 R299 A380 W381
BS05 ATQ B V338 W358 E363 V270 W290 E295 MOAD: Ki=0.35uM
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:1d1w, PDBe:1d1w, PDBj:1d1w
PDBsum1d1w
PubMed11051558
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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