Structure of PDB 3jwt Chain A

Receptor sequence

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

RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW

3D structure

• PDB: 3jwt Unexpected binding modes of nitric oxide synthase inhibitors effective in the prevention of a cerebral palsy phenotype in an animal model.
• Chain: A
• Resolution: 2.01 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 V416 F584 W587 W678 F704	W100 C106 V107 F275 W278 W369 F395
BS02	H4B	A	S334 R596 V677 W678	S36 R287 V368 W369
BS03	JI5	A	Q478 P565 V567 S585 G586 E592 W678 Y706	Q169 P256 V258 S276 G277 E283 W369 Y397	MOAD: Ki=5.3nM BindingDB: Ki=14nM
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:3jwt, PDBe:3jwt, PDBj:3jwt
• PDBsum: 3jwt
• PubMed: 20337441
• UniProt: P29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)