Structure of PDB 2nos Chain A

Receptor sequence
>2nosA (length=322) Species: 10090 (Mus musculus) [Search protein sequence]
NPKSLTRGPRDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVT
KEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTA
QEMFQHICRHILYATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGY
QMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFE
IPPDLVLEVTMELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIG
VRDFCDTQDRAVTEINVAVLHSFQKQNVTIMDHHTASESFMKHMQNEVLS
PFYYYQIEPWKTHIWQNEHHHH
3D structure
PDB2nos The structure of nitric oxide synthase oxygenase domain and inhibitor complexes.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C194 R197 W366 E371
Catalytic site (residue number reindexed from 1) C80 R83 W243 E248
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 W188 A191 R193 C194 I195 G196 S236 F363 N364 G365 W366 M368 Y483 Y485 W74 A77 R79 C80 I81 G82 S122 F240 N241 G242 W243 M245 Y303 Y305
BS02 AGU A W366 Y367 M368 E371 W243 Y244 M245 E248 BindingDB: IC50=26550nM
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2nos, PDBe:2nos, PDBj:2nos
PDBsum2nos
PubMed9334294
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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