Structure of PDB 1d1v Chain B

Receptor sequence

>1d1vB (length=414) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW

3D structure

• PDB: 1d1v Implications for isoform-selective inhibitor design derived from the binding mode of bulky isothioureas to the heme domain of endothelial nitric-oxide synthase.
• Chain: B
• Resolution: 1.93 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	H4B	B	W447 F462 H463 E465	W379 F394 H395 E397
BS03	HEM	B	W180 R185 C186 F355 S356 W358 E363 W449 F475 Y477	W112 R117 C118 F287 S288 W290 E295 W381 F407 Y409
BS04	H4B	B	S104 R367 A448 W449	S36 R299 A380 W381
BS05	PTU	B	P336 V338 F355 W358 E363	P268 V270 F287 W290 E295

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1d1v, PDBe:1d1v, PDBj:1d1v
• PDBsum: 1d1v
• PubMed: 11331290
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)