Structure of PDB 2nsi Chain A

Receptor sequence

>2nsiA (length=420) Species: 9606 (Homo sapiens)

RHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDK
PTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLT
GDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVR
YSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPA
NVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAME
HPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRD
FCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVT
IMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLN
YVLSPFYYYQVEAWKTHVWQ

3D structure

• PDB: 2nsi Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase.
• Chain: A
• Resolution: 3.0 Å

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	HEM	A	W194 C200 I201 G202 F369 N370 G371 W372 E377 W463 Y491	W112 C118 I119 G120 F287 N288 G289 W290 E295 W381 Y409
BS02	H4B	A	S118 M120 R381 I462 W463	S36 M38 R299 I380 W381
BS03	ITU	A	P350 W372 E377	P268 W290 E295	BindingDB: IC50=160nM
BS04	H4B	A	F476 H477 Q478	F394 H395 Q396

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:2nsi, PDBe:2nsi, PDBj:2nsi
• PDBsum: 2nsi
• PubMed: 10409685
• UniProt: P35228|NOS2_HUMAN Nitric oxide synthase, inducible (Gene Name=NOS2)