Structure of PDB 3jx6 Chain B

Receptor sequence

>3jx6B (length=411) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEAQ
PDPWNTHVWKG

3D structure

• PDB: 3jx6 Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model.
• Chain: B
• Resolution: 2.35 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 C415 M570 F584 W587 E592 F704	W102 C108 M263 F277 W280 E285 F397
BS04	H4B	B	S334 R596 V677 W678	S36 R289 V370 W371
BS05	JI5	B	V336 P565 E592 W678	V38 P258 E285 W371	MOAD: Ki=2180nM BindingDB: Ki=14nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:3jx6, PDBe:3jx6, PDBj:3jx6
• PDBsum: 3jx6
• PubMed: 20337441
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)