Structure of PDB 5fvp Chain A

Receptor sequence
>5fvpA (length=407) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPTKDQLFPLAK
EFLDQYYSSIKRFGSKAHMDRLEEVNKEIESTSTYQLKDTELIYGAKHAW
RNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAI
TIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQG
WKAPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFDWFKDLGL
KWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEE
VAKKMDLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFI
KHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPD
PWNTHVW
3D structure
PDB5fvp Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibition by Optimization of the 2-Aminopyridine-Based Scaffold with a Pyridine Linker.
ChainA
Resolution2.099 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 V416 F584 W587 W678 F704 Y706 W100 C106 V107 F275 W278 W369 F395 Y397
BS02 H4B A R596 V677 W678 R287 V368 W369
BS03 WOS A V567 N569 S585 W587 E592 V258 N260 S276 W278 E283 MOAD: Ki=547nM
BindingDB: Ki=547nM
BS04 H4B A F691 H692 Q693 E694 F382 H383 Q384 E385
BS05 ZN A C326 C331 C28 C33
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:5fvp, PDBe:5fvp, PDBj:5fvp
PDBsum5fvp
PubMed27050842
UniProtP29476|NOS1_RAT Nitric oxide synthase 1 (Gene Name=Nos1)

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