Structure of PDB 3e68 Chain A

Receptor sequence
>3e68A (length=415) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSDFTSCLGSIMNPKSLTRGPRDKPTPL
EELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDEL
IFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATN
NGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEF
TQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKY
EWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDT
QRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDH
HTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLS
PFYYYQIEPWKTHIW
3D structure
PDB3e68 Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
ChainA
Resolution2.2 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) C114 R117 W286 E291
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 AT6 A R260 P344 V346 W366 E371 R382 R180 P264 V266 W286 E291 R302 MOAD: ic50=0.12uM
BS02 HEM A W188 C194 S236 F363 G365 W366 E371 W457 Y485 W108 C114 S156 F283 G285 W286 E291 W377 Y405
BS03 H4B A S112 R375 I456 W457 S32 R295 I376 W377
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:3e68, PDBe:3e68, PDBj:3e68
PDBsum3e68
PubMed18849972
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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