Structure of PDB 1d1w Chain A

Receptor sequence
>1d1wA (length=416) Species: 9913 (Bos taurus) [Search protein sequence]
GPKFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLQTRPS
PGPPPAEQLLSQARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYH
LRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNH
IKYATNRGNLRSAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGD
PANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVP
LEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGT
RNLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAK
VTIVDHHAATVSFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEM
VNYILSPAFRYQPDPW
3D structure
PDB1d1w Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas.
ChainA
Resolution2.0 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) C120 R123 W292 E297
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 S228 M341 F355 S356 W358 E363 W449 F475 Y477 W114 C120 S162 M275 F289 S290 W292 E297 W383 F409 Y411
BS03 H4B A S104 R367 A448 W449 S38 R301 A382 W383
BS04 ATQ A P336 V338 W358 E363 P270 V272 W292 E297 MOAD: Ki=0.35uM
BS05 H4B A W447 F462 W381 F396
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1d1w, PDBe:1d1w, PDBj:1d1w
PDBsum1d1w
PubMed11051558
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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