Structure of PDB 3nlo Chain B

Receptor sequence

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

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVATKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG

3D structure

• PDB: 3nlo Exploration of the Active Site of Neuronal Nitric Oxide Synthase by the Design and Synthesis of Pyrrolidinomethyl 2-Aminopyridine Derivatives.
• Chain: B
• Resolution: 2.3 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 E694	F384 H385 Q386 E387
BS02	ZN	B	C326 C331	C28 C33
BS03	HEM	B	W409 C415 G417 F584 W587 E592 W678 F704 Y706	W102 C108 G110 F277 W280 E285 W371 F397 Y399
BS04	H4B	B	S334 M336 R596 V677 W678	S36 M38 R289 V370 W371
BS05	JSR	B	M336 Q478 P565 V567 S585 W587 E592	M38 Q171 P258 V260 S278 W280 E285	BindingDB: Ki=18060000nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

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