Structure of PDB 3dqs Chain B

Receptor sequence

>3dqsB (length=402) Species: 9913 (Bos taurus)

KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRAEQLLSQAR
DFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFM
KHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPD
PW

3D structure

• PDB: 3dqs Crystal structures of constitutive nitric oxide synthases in complex with de novo designed inhibitors.
• Chain: B
• Resolution: 2.03 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C186 R189 W358 E363
• Catalytic site (residue number reindexed from 1): C106 R109 W278 E283
• 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	B	C96 C101	C28 C33
BS02	H4B	B	W447 F462	W367 F382
BS03	HEM	B	W180 R185 C186 S228 F355 W358 E363 W449 F475 Y477	W100 R105 C106 S148 F275 W278 E283 W369 F395 Y397
BS04	H4B	B	S104 R367 A448 W449	S36 R287 A368 W369
BS05	JI3	B	L107 P336 W358 E363	L39 P256 W278 E283	MOAD: Ki=85.2uM BindingDB: Ki=85000nM

Gene Ontology

Molecular Function

• GO:0004517 nitric-oxide synthase activity
• GO:0020037 heme binding

Biological Process

• GO:0006809 nitric oxide biosynthetic process

External links

• PDB: RCSB:3dqs, PDBe:3dqs, PDBj:3dqs
• PDBsum: 3dqs
• PubMed: 19296678
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)