Structure of PDB 1rs9 Chain A

Receptor sequence
>1rs9A (length=406) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRPPAEQLL
SQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGA
KQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNL
RSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELC
IQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFA
ALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYN
ILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAAT
VSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFR
YQPDPW
3D structure
PDB1rs9 Structures of the neuronal and endothelial nitric oxide synthase heme domain with D-nitroarginine-containing dipeptide inhibitors bound.
ChainA
Resolution2.22 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C110 R113 W282 E287
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 A W180 C186 F355 S356 W358 E363 W449 Y477 W104 C110 F279 S280 W282 E287 W373 Y401
BS02 H4B A R367 A448 W449 R291 A372 W373
BS03 D7P A V106 Q249 R252 V338 F355 S356 G357 W358 E363 Y477 V40 Q173 R176 V262 F279 S280 G281 W282 E287 Y401
BS04 ZN A C96 C101 C30 C35
BS05 H4B A W447 F462 W371 F386
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
GO:0020037 heme binding
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1rs9, PDBe:1rs9, PDBj:1rs9
PDBsum1rs9
PubMed15122883
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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