Structure of PDB 3nle Chain B

Receptor sequence

>3nleB (length=401) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPAEQLLSQARD
FINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAWR
NAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAIT
VFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHGW
TPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGLR
WYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILEDV
AVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFMK
HLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPDP
W

3D structure

• PDB: 3nle Exploration of the Active Site of Neuronal Nitric Oxide Synthase by the Design and Synthesis of Pyrrolidinomethyl 2-Aminopyridine Derivatives.
• 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): C105 R108 W277 E282
• 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	H4B	B	F462 H463 Q464	F381 H382 Q383
BS02	ZN	B	C96 C101	C28 C33
BS03	HEM	B	W180 C186 V187 M341 F355 W358 E363 F475	W99 C105 V106 M260 F274 W277 E282 F394
BS04	H4B	B	R367 A448 W449	R286 A367 W368
BS05	JRR	B	L107 Q249 P336 W358 E363 Y477	L39 Q168 P255 W277 E282 Y396	MOAD: Ki=19.2uM BindingDB: Ki=19200nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:3nle, PDBe:3nle, PDBj:3nle
• PDBsum: 3nle
• PubMed: 20958055
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)