Structure of PDB 1m8d Chain A

Receptor sequence
>1m8dA (length=416) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSDKSCLGSIMNPKSLTRGPRDKPTPLE
ELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELI
FATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNN
GNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFT
QLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYE
WFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQ
RYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHH
TASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSP
FYYYQIEPWKTHIWQN
3D structure
PDB1m8d Conformational Changes in Nitric Oxide Synthases Induced by Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency
ChainA
Resolution2.35 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) C113 R116 W285 E290
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 C194 F363 N364 G365 W366 E371 W457 Y483 Y485 W107 C113 F282 N283 G284 W285 E290 W376 Y402 Y404
BS02 H4B A S112 M114 R375 I456 W457 S31 M33 R294 I375 W376
BS03 CLW A P344 F363 N364 W366 Y367 P263 F282 N283 W285 Y286 MOAD: Kd~4.3uM
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:1m8d, PDBe:1m8d, PDBj:1m8d
PDBsum1m8d
PubMed12437348
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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