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BioLiP

Structure of PDB 1m8e Chain B

Receptor sequence
>1m8eB (length=411) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSCLGSIMNPKSLTRGPRDKPTPLEELL
PHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFAT
KMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNI
RSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLC
IDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWFQ
ELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYN
ILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTAS
ESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYY
YQIEPWKTHIW
3D structure
PDB1m8e Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
ChainB
Resolution2.9 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) C110 R113 W282 E287
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 S236 F363 N364 G365 W366 W457 Y485 W104 C110 S152 F279 N280 G281 W282 W373 Y401
BS02 H4B B S112 R375 I456 W457 S28 R291 I372 W373
BS03 7NI B P344 G365 W366 Y367 E371 P260 G281 W282 Y283 E287 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:1m8e, PDBe:1m8e, PDBj:1m8e
PDBsum1m8e
PubMed12437348
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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