Structure of PDB 1d0o Chain B

Receptor sequence

>1d0oB (length=414) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW

3D structure

• PDB: 1d0o Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism.
• Chain: B
• Resolution: 1.95 Å

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	INE	B	S104 V106 R367 A448 W449	S36 V38 R299 A380 W381	BindingDB: IC50=2000nM
BS03	INE	B	W447 F462 H463 Q464 E465	W379 F394 H395 Q396 E397	BindingDB: IC50=2000nM
BS04	HEM	B	W180 R185 C186 F355 S356 W358 W449 F475 Y477	W112 R117 C118 F287 S288 W290 W381 F407 Y409
BS05	INE	B	P336 F355 S356 G357 W358 Y359 E363	P268 F287 S288 G289 W290 Y291 E295	BindingDB: IC50=2000nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1d0o, PDBe:1d0o, PDBj:1d0o
• PDBsum: 1d0o
• PubMed: 11695891
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)