Structure of PDB 3e6t Chain B

Receptor sequence
>3e6tB (length=410) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATCLGSIMNPKSLTRGPRDKPTPLEELLP
HAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFATK
MAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGNIR
SAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQLCI
DLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWFQE
LGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRYNI
LEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTASE
SFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFYYY
QIEPWKTHIW
3D structure
PDB3e6t Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
ChainB
Resolution2.5 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 F363 G365 W366 E371 W457 Y483 Y485 W103 C109 F278 G280 W281 E286 W372 Y398 Y400
BS02 H4B B R375 I456 W457 R290 I371 W372
BS03 1A2 B Q257 R260 Y341 P344 V346 G365 W366 E371 R382 Q172 R175 Y256 P259 V261 G280 W281 E286 R297 MOAD: ic50=1.2uM
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:3e6t, PDBe:3e6t, PDBj:3e6t
PDBsum3e6t
PubMed18849972
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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