Structure of PDB 5ago Chain B

Receptor sequence
>5agoB (length=411) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPVRTKDQLFPL
AKEFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKH
AWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRS
AITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQ
QGWKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDL
GLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNIL
EEVAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATES
FIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQ
PDPWNTHVWKG
3D structure
PDB5ago Mechanism of Inactivation of Neuronal Nitric Oxide Synthase by (S)-2-Amino-5-(2-(Methylthio)Acetimidamido)Pentanoic Acid.
ChainB
Resolution1.902 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 H4B B F691 H692 E694 F384 H385 E387
BS02 ZN B C326 C331 C28 C33
BS03 HEM B W409 C415 F584 W587 E592 W678 F704 Y706 W102 C108 F277 W280 E285 W371 F397 Y399
BS04 H4B B S334 R596 V677 W678 S36 R289 V370 W371
BS05 VUR B Q478 P565 S585 Y588 E592 D597 Q171 P258 S278 Y281 E285 D290 MOAD: Ki=0.42uM
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5ago, PDBe:5ago, PDBj:5ago
PDBsum5ago
PubMed25874809
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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