Structure of PDB 4cx7 Chain C

Receptor sequence

>4cx7C (length=413) Species: 9606 (Homo sapiens)

RHVRIKNWGSGMTFQDTLHHKAKGICLGSIMTPKSLTRGPRDKPTPPDEL
LPQAIEFVNQYYGSFKEAKIEEHLARVEAVTKEIETTGTYQLTGDELIFA
TKQAWRNAPRCIGRIQWSNLQVFDARSCSTAREMFEHICRHVRYSTNNGN
IRSAITVFPQRSDGKHDFRVWNAQLIRYAGYQMPDGSIRGDPANVEFTQL
CIDLGWKPKYGRFDVVPLVLQANGRDPELFEIPPDLVLEVAMEHPKYEWF
RELELKWYALPAVANMLLEVGGLEFPGCPFNGWYMGTEIGVRDFCDVQRY
NILEEVGRRMGLETHKLASLWKDQAVVEINIAVLHSFQKQNVTIMDHHSA
AESFMKYMQNEYRSRGGCPADWIWLVPPMSGSITPVFHQEMLNYVLSPFY
YYQVEAWKTHVWQ

3D structure

• PDB: 4cx7 Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.
• Chain: C
• Resolution: 3.16 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C200 R203 W372 E377
• Catalytic site (residue number reindexed from 1): C111 R114 W283 E288
• 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	C	W194 C200 I201 F369 G371 W372 E377 W463 Y489 Y491	W105 C111 I112 F280 G282 W283 E288 W374 Y400 Y402
BS02	H4B	C	M120 R381 I462 W463	M31 R292 I373 W374
BS03	S71	C	M120 Q263 P350 V352 W372 E377 W463 Y491	M31 Q174 P261 V263 W283 E288 W374 Y402	BindingDB: Ki=6629nM
BS04	H4B	C	F476 H477 Q478	F387 H388 Q389

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:4cx7, PDBe:4cx7, PDBj:4cx7
• PDBsum: 4cx7
• PubMed: 25089924
• UniProt: P35228|NOS2_HUMAN Nitric oxide synthase, inducible (Gene Name=NOS2)