Structure of PDB 4luw Chain A

Receptor sequence
>4luwA (length=405) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRPAEQLLS
QARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAK
QAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLR
SAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCI
QHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAA
LGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNI
LEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATV
SFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRY
QPDPW
3D structure
PDB4luw Structural and biological studies on bacterial nitric oxide synthase inhibitors.
ChainA
Resolution2.25 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) 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 HEM A W180 C186 G188 S228 F355 W358 E363 W449 F475 Y477 W103 C109 G111 S151 F278 W281 E286 W372 F398 Y400
BS02 H4B A S104 R367 A448 W449 S38 R290 A371 W372
BS03 QJ8 A P336 V338 N340 F355 W358 E363 Y477 P259 V261 N263 F278 W281 E286 Y400 MOAD: Kd=2.1uM
BindingDB: Ki=2179nM
BS04 ZN A C96 C101 C30 C35
BS05 H4B A W447 F462 W370 F385
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4luw, PDBe:4luw, PDBj:4luw
PDBsum4luw
PubMed24145412
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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