Structure of PDB 3e65 Chain B

Receptor sequence
>3e65B (length=421) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDK
PTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLT
LDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHIL
YATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAA
TLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTME
HPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVT
IMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLN
YVLSPFYYYQIEPWKTHIWQN
3D structure
PDB3e65 Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
ChainB
Resolution2.05 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) C118 R121 W290 E295
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 F363 G365 W366 E371 W457 Y483 Y485 W112 C118 Q123 F287 G289 W290 E295 W381 Y407 Y409
BS02 H4B B S112 M114 R375 I456 W457 S36 M38 R299 I380 W381
BS03 XXZ B Q257 R260 Y341 P344 V346 G365 W366 E371 R382 Q181 R184 Y265 P268 V270 G289 W290 E295 R306 MOAD: ic50=0.13uM
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:3e65, PDBe:3e65, PDBj:3e65
PDBsum3e65
PubMed18849972
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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