Structure of PDB 1q2o Chain A

Receptor sequence

>1q2oA (length=405) Species: 9913 (Bos taurus)

GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPPPAEQLLS
QARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAK
QAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLR
SAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCI
QHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAA
LGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRDLCDPHRYNI
LEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATV
SFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRY
QPDPW

3D structure

• PDB: 1q2o Structural basis for dipeptide amide isoform-selective inhibition of neuronal nitric oxide synthase.
• Chain: A
• Resolution: 1.74 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): C186 R189 W358 E363
• Catalytic site (residue number reindexed from 1): C109 R112 W281 E286
• 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	A	C96 C101	C30 C35
BS02	HEM	A	W180 C186 F355 W358 E363 W449 F475 Y477	W103 C109 F278 W281 E286 W372 F398 Y400
BS03	H4B	A	S104 R367 A448 W449	S38 R290 A371 W372
BS04	DP1	A	S248 Q249 R252 V338 S356 G357 W358 E363	S171 Q172 R175 V261 S279 G280 W281 E286	MOAD: Ki=9.5uM
BS05	H4B	A	W447 F462 E465	W370 F385 E388

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:1q2o, PDBe:1q2o, PDBj:1q2o
• PDBsum: 1q2o
• PubMed: 14718923
• UniProt: P29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)