Structure of PDB 3n66 Chain A

Receptor sequence
>3n66A (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNHRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW
3D structure
PDB3n66 Role of zinc in isoform-selective inhibitor binding to neuronal nitric oxide synthase .
ChainA
Resolution1.78 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 S585 W587 E592 R596 W678 F704 Y706 W100 C106 F275 S276 W278 E283 R287 W369 F395 Y397
BS02 XFN A M336 F584 W587 E592 R596 W678 M38 F275 W278 E283 R287 W369 BindingDB: Ki=85nM
BS03 ZN A C326 C331 C28 C33
BS04 CL A Y588 D597 Y279 D288
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3n66, PDBe:3n66, PDBj:3n66
PDBsum3n66
PubMed21138269
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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