Structure of PDB 5unu Chain B

Receptor sequence

>5unuB (length=411) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG

3D structure

• PDB: 5unu Nitrile in the Hole: Discovery of a Small Auxiliary Pocket in Neuronal Nitric Oxide Synthase Leading to the Development of Potent and Selective 2-Aminoquinoline Inhibitors.
• Chain: B
• Resolution: 2.05 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C108 R111 W280 E285
• 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	F691 H692 Q693	F384 H385 Q386
BS02	ZN	B	C326 C331	C28 C33
BS03	HEM	B	W409 R414 C415 F584 W587 E592 W678 F704 Y706	W102 R107 C108 F277 W280 E285 W371 F397 Y399
BS04	H4B	B	S334 M336 R596 V677 W678	S36 M38 R289 V370 W371
BS05	8EY	B	P565 V567 N569 S585 W587 E592 Y706	P258 V260 N262 S278 W280 E285 Y399	MOAD: Ki=0.033uM BindingDB: Ki=33nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:5unu, PDBe:5unu, PDBj:5unu
• PDBsum: 5unu
• PubMed: 28422508
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)