Structure of PDB 3n63 Chain B

Receptor sequence
>3n63B (length=411) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIVLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRNYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG
3D structure
PDB3n63 Role of zinc in isoform-selective inhibitor binding to neuronal nitric oxide synthase .
ChainB
Resolution2.0 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) 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 ZN B C326 C331 C28 C33
BS02 HEM B W409 R414 C415 F584 W587 E592 R596 W678 F704 Y706 W102 R107 C108 F277 W280 E285 R289 W371 F397 Y399
BS03 XFN B F584 W587 E592 R596 W678 F277 W280 E285 R289 W371 BindingDB: Ki=85nM
BS04 CL B Y588 N597 Y281 N290
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:3n63, PDBe:3n63, PDBj:3n63
PDBsum3n63
PubMed21138269
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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