Structure of PDB 2oro Chain A

Receptor sequence
>2oroA (length=313) Species: 10090 (Mus musculus) [Search protein sequence]
MNPKSLTRGPRDKPTPLEELLPHAIEFINQYYGSFKEAKIEEHLARLEAV
TKEIETTGTYQLTLDELIFATKMAWRNAPRCIGRIQWSNLQVFDARNCST
AQEMFQHICRHILYATNNGNIRSAITVFPQRSDGKHDFRLWNSQLIRYAG
YQMPDGTIRGDAATLEFTQLCIDLGWKPRYGRFDVLPLVLQADGQDPEVF
EIPPDLVLEVTMEYEWFQELGLKWYALPAVANMLLEVGGLEFPACPFNGW
YMGNILEEINVAVLHSFQKQNVTIMDHHTASESFMKHMQNEYVLSPFYYY
QIEPWKTHIWQNE
3D structure
PDB2oro Design, Synthesis, and Activity of 2-Imidazol-1-ylpyrimidine Derived Inducible Nitric Oxide Synthase Dimerization Inhibitors
ChainA
Resolution2.0 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
Catalytic site (residue number reindexed from 1) C81 R84 W250
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 A W188 R193 C194 G196 L203 F363 G365 W366 M368 Y483 Y485 W75 R80 C81 G83 L90 F247 G249 W250 M252 Y298 Y300
BS02 228 A Q257 P344 V346 Y367 M368 Q144 P228 V230 Y251 M252 MOAD: ic50=0.29nM
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:2oro, PDBe:2oro, PDBj:2oro
PDBsum2oro
PubMed17315988
UniProtP29477|NOS2_MOUSE Nitric oxide synthase, inducible (Gene Name=Nos2)

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