Structure of PDB 4cx1 Chain B

Receptor sequence

>4cx1B (length=404) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKPAEQLLSQ
ARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQ
AWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRS
AITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQ
HGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAAL
GLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNIL
EDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVS
FMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQ
PDPW

3D structure

• PDB: 4cx1 Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.
• Chain: B
• Resolution: 2.13 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C186 R189 W358 E363
• Catalytic site (residue number reindexed from 1): C108 R111 W280 E285
• 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	H2B	B	W447 F462 Q464 E465	W369 F384 Q386 E387
BS02	HEM	B	W180 C186 V187 G188 S228 M341 F355 W358 E363 W449 F475 Y477	W102 C108 V109 G110 S150 M263 F277 W280 E285 W371 F397 Y399
BS03	H2B	B	S104 R367 A448 W449	S36 R289 A370 W371
BS04	HW9	B	V338 M341 F355 W358 E363 W449 Y477	V260 M263 F277 W280 E285 W371 Y399	BindingDB: Kd=5.58e+4nM
BS05	ZN	B	C96 C101	C28 C33

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:4cx1, PDBe:4cx1, PDBj:4cx1
• PDBsum: 4cx1
• PubMed: 25089924
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)