Structure of PDB 3nln Chain A

Receptor sequence

>3nlnA (length=407) Species: 10116 (Rattus norvegicus)

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW

3D structure

• PDB: 3nln Exploration of the Active Site of Neuronal Nitric Oxide Synthase by the Design and Synthesis of Pyrrolidinomethyl 2-Aminopyridine Derivatives.
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C415 R418 W587 E592
• Catalytic site (residue number reindexed from 1): C106 R109 W278 E283
• 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	HEM	A	W409 R414 C415 F584 W587 F704 Y706	W100 R105 C106 F275 W278 F395 Y397
BS02	H4B	A	S334 R596 V677 W678	S36 R287 V368 W369
BS03	JRS	A	M336 L337 P565 V567 F584 W587 E592 Y706	M38 L39 P256 V258 F275 W278 E283 Y397	BindingDB: Ki=18710000nM
BS04	ZN	A	C326 C331	C28 C33
BS05	H4B	A	F691 E694	F382 E385

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

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