Structure of PDB 1fop Chain A

Receptor sequence

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

GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPS
PGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYH
LRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNH
IKYATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGD
PANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVP
LEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGT
RNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAK
VTIVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEM
VNYILSPAFRYQPDPW

3D structure

• PDB: 1fop Crystallographic studies on endothelial nitric oxide synthase complexed with nitric oxide and mechanism-based inhibitors.
• Chain: A
• Resolution: 2.3 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	HEM	A	W180 C186 G188 M341 F355 S356 W358 E363 W449 F475 Y477	W114 C120 G122 M275 F289 S290 W292 E297 W383 F409 Y411
BS02	H4B	A	S104 R367 A448 W449	S38 R301 A382 W383
BS03	ARG	A	Q249 P336 W358 Y359 E363 N368	Q183 P270 W292 Y293 E297 N302
BS04	ZN	A	C96 C101	C30 C35
BS05	H4B	A	W447 F462	W381 F396

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1fop, PDBe:1fop, PDBj:1fop
• PDBsum: 1fop
• PubMed: 11331003
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)