Structure of PDB 1nsi Chain C

Receptor sequence

>1nsiC (length=420) Species: 9606 (Homo sapiens)

RHVRIKNWGSGMTFQDTLHHKAKGILTCRSKSCLGSIMTPKSLTRGPRDK
PTPPDELLPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLT
GDELIFATKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVR
YSTNNGNIRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPA
NVEFTQLCIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAME
HPKYEWFRELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRD
FCDVQRYNILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVT
IMDHHSAAESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLN
YVLSPFYYYQVEAWKTHVWQ

3D structure

• PDB: 1nsi 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: C
• Resolution: 2.55 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	ZN	C	C110 C115	C28 C33
BS02	HEM	C	W194 C200 G202 F369 N370 G371 W372 E377 W463 Y491	W112 C118 G120 F287 N288 G289 W290 E295 W381 Y409
BS03	H4B	C	S118 R381 I462 W463	S36 R299 I380 W381
BS04	ARG	C	W372 Y373 E377 D382	W290 Y291 E295 D300
BS05	H4B	C	F476 Q478 E479	F394 Q396 E397

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:1nsi, PDBe:1nsi, PDBj:1nsi
• PDBsum: 1nsi
• PubMed: 10409685
• UniProt: P35228|NOS2_HUMAN Nitric oxide synthase, inducible (Gene Name=NOS2)