Structure of PDB 3ebd Chain B

Receptor sequence
>3ebdB (length=421) Species: 10090 (Mus musculus) [Search protein sequence]
QYVRIKNWGSGEILHDTLHHKATSDFTCKSKSCLGSIMNPKSLTRGPRDK
PTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAVTKEIETTGTYQLT
LDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCSTAQEMFQHICRHIL
YATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAGYQMPDGTIRGDAA
TLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVFEIPPDLVLEVTME
HPKYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGWYMGTEIGVRD
FCDTQRYNILEEVGRRMGLETHTLASLWKDRAVTEINVAVLHSFQKQNVT
IMDHHTASESFMKHMQNEYRARGGCPADWIWLVPPVSGSITPVFHQEMLN
YVLSPFYYYQIEPWKTHIWQN
3D structure
PDB3ebd Anchored plasticity opens doors for selective inhibitor design in nitric oxide synthase.
ChainB
Resolution2.4 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 L203 S236 F363 N364 G365 W366 E371 W457 Y485 W112 C118 L127 S160 F287 N288 G289 W290 E295 W381 Y409
BS02 H4B B S112 M114 R375 I456 W457 S36 M38 R299 I380 W381
BS03 329 B P344 A345 V346 F363 N364 E371 P268 A269 V270 F287 N288 E295 MOAD: ic50=0.04uM
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:3ebd, PDBe:3ebd, PDBj:3ebd
PDBsum3ebd
PubMed18849972
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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