Structure of PDB 3nlj Chain B

Receptor sequence

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

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEAQ
PDPWNTHVWKG

3D structure

• PDB: 3nlj Exploration of the Active Site of Neuronal Nitric Oxide Synthase by the Design and Synthesis of Pyrrolidinomethyl 2-Aminopyridine Derivatives.
• Chain: B
• Resolution: 2.2 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 Q693	F384 Q386
BS02	HEM	B	W409 C415 M570 F584 S585 W587 E592 W678 F704	W102 C108 M263 F277 S278 W280 E285 W371 F397
BS03	H4B	B	S334 R596 V677 W678	S36 R289 V370 W371
BS04	JRR	B	Q478 V567 S585 W587 E592 W678	Q171 V260 S278 W280 E285 W371	BindingDB: Ki=7.0nM,IC50=100nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:3nlj, PDBe:3nlj, PDBj:3nlj
• PDBsum: 3nlj
• PubMed: 20958055
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)