Structure of PDB 1ed4 Chain A

Receptor sequence

>1ed4A (length=416) Species: 9913 (Bos taurus)

GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPS
PGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYH
LRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNH
IKYATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGD
PANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVP
LEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGT
RNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAK
VTIVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEM
VNYILSPAFRYQPDPW

3D structure

• PDB: 1ed4 Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
• Chain: A
• Resolution: 1.86 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C186 R189 W358 E363
• Catalytic site (residue number reindexed from 1): C120 R123 W292 E297
• 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	A	C96 C101	C30 C35
BS02	HEM	A	W180 C186 F355 S356 W358 E363 W449 F475 Y477	W114 C120 F289 S290 W292 E297 W383 F409 Y411
BS03	IPU	A	P336 V338 F355 W358 E363	P270 V272 F289 W292 E297	MOAD: Ki=0.022uM
BS04	IPU	A	W447 F462	W381 F396	MOAD: Ki=0.022uM
BS05	IPU	A	A448 W449	A382 W383	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)