Structure of PDB 1m8h Chain B

Receptor sequence
>1m8hB (length=412) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATCLGSIMNPKSLTRGPRDKPTPLEELLP
HAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATK
MAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIR
SAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCI
DLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWFQE
LGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYNI
LEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTASE
SFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYY
QIEPWKTHIWQN
3D structure
PDB1m8h Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
ChainB
Resolution2.85 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) C109 R112 W281 E286
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 B W188 C194 I195 S236 F363 N364 W366 E371 W457 Y485 W103 C109 I110 S151 F278 N279 W281 E286 W372 Y400
BS02 H4B B S112 R375 I456 W457 S27 R290 I371 W372
BS03 6NI B P344 N364 W366 Y367 E371 P259 N279 W281 Y282 E286 BindingDB: IC50=20000nM
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:1m8h, PDBe:1m8h, PDBj:1m8h
PDBsum1m8h
PubMed12437348
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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