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BioLiP

Structure of PDB 3e7g Chain A

Receptor sequence
>3e7gA (length=421) Species: 9606 (Homo sapiens) [Search protein sequence]
RHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDK
PTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLT
GDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVR
YSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPA
NVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAME
HPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRD
FCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVT
IMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLN
YVLSPFYYYQVEAWKTHVWQD
3D structure
PDB3e7g 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) C200 R203 W372 E377
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 ZN A C110 C115 C28 C33
BS02 HEM A W194 C200 F369 G371 W372 E377 W463 Y489 Y491 W112 C118 F287 G289 W290 E295 W381 Y407 Y409
BS03 H4B A M120 I462 W463 M38 I380 W381
BS04 AT2 A Q263 R266 Y347 P350 F369 E377 R388 Q181 R184 Y265 P268 F287 E295 R306 MOAD: ic50=0.35uM
BindingDB: IC50=350nM
BS05 H4B A F476 H477 F394 H395
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:3e7g, PDBe:3e7g, PDBj:3e7g
PDBsum3e7g
PubMed18849972
UniProtP35228|NOS2_HUMAN Nitric oxide synthase, inducible (Gene Name=NOS2)

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