Structure of PDB 1ed4 Chain B

Receptor sequence

>1ed4B (length=414) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPSPG
PPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLR
ESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIK
YATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPA
NVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLE
HPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRN
LCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVT
IVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVN
YILSPAFRYQPDPW

3D structure

• PDB: 1ed4 Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
• Chain: B
• Resolution: 1.86 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	IPU	B	A448 W449	A380 W381	MOAD: Ki=0.022uM
BS03	IPU	B	W447 F462 H463	W379 F394 H395	MOAD: Ki=0.022uM
BS04	HEM	B	W180 C186 F355 S356 W358 E363 W449 F475 Y477	W112 C118 F287 S288 W290 E295 W381 F407 Y409
BS05	IPU	B	P336 F355 W358 E363	P268 F287 W290 E295	MOAD: Ki=0.022uM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1ed4, PDBe:1ed4, PDBj:1ed4
• PDBsum: 1ed4
• PubMed: 11051558
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)