Structure of PDB 3e7t Chain B

Receptor sequence
>3e7tB (length=413) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSSCLGSIMNPKSLTRGPRDKPTPLEEL
LPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLTLDELIFA
TKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHILYATNNGN
IRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAATLEFTQL
CIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTMEHPKYEWF
QELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRDFCDTQRY
NILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVTIMDHHTA
SESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLNYVLSPFY
YYQIEPWKTHIWQ
3D structure
PDB3e7t Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
ChainB
Resolution2.6 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) C111 R114 W283 E288
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 Q199 S236 M349 F363 G365 W366 E371 W457 Y485 W105 C111 Q116 S153 M266 F280 G282 W283 E288 W374 Y402
BS02 HBI B M114 R375 I456 W457 M31 R292 I373 W374
BS03 B14 B Q257 R260 Y341 P344 V346 G365 W366 E371 R382 Q174 R177 Y258 P261 V263 G282 W283 E288 R299
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:3e7t, PDBe:3e7t, PDBj:3e7t
PDBsum3e7t
PubMed18849972
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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