Structure of PDB 3jx1 Chain B

Receptor sequence

>3jx1B (length=410) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWK

3D structure

• PDB: 3jx1 Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model.
• Chain: B
• Resolution: 2.0 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 E694	F384 E387
BS02	ZN	B	C326 C331	C28 C33
BS03	HEM	B	W409 C415 M570 F584 W587 W678 F704	W102 C108 M263 F277 W280 W371 F397
BS04	H4B	B	S334 M336 R596 V677 W678	S36 M38 R289 V370 W371
BS05	JI5	B	P565 S585 G586 E592 W678 Y706	P258 S278 G279 E285 W371 Y399	MOAD: Ki=290nM 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:3jx1, PDBe:3jx1, PDBj:3jx1
• PDBsum: 3jx1
• PubMed: 20337441
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)