Structure of PDB 3jwv Chain A

Receptor sequence

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

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW

3D structure

• PDB: 3jwv Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model.
• Chain: A
• Resolution: 1.98 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 C415 F584 W587 F704 Y706	W100 C106 F275 W278 F395 Y397
BS02	H4B	A	S334 M336 R596 V677 W678	S36 M38 R287 V368 W369
BS03	J14	A	M336 Q478 V567 F584 S585 W587 E592	M38 Q169 V258 F275 S276 W278 E283	MOAD: Ki=18.9nM BindingDB: Ki=26600000nM
BS04	ZN	A	C326 C331	C28 C33
BS05	H4B	A	F691 H692 Q693 E694	F382 H383 Q384 E385

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

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