Structure of PDB 4cx0 Chain B

Receptor sequence
>4cx0B (length=403) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRPAEQLLSQA
RDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQA
WRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSA
ITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQH
GWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALG
LRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILE
DVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSF
MKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRAQP
DPW
3D structure
PDB4cx0 Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C186 R189 W358 E363
Catalytic site (residue number reindexed from 1) C107 R110 W279 E284
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 H4B B W447 F462 E465 W368 F383 E386
BS02 ZN B C96 C101 C28 C33
BS03 HEM B W180 C186 V187 F355 W358 E363 W449 F475 W101 C107 V108 F276 W279 E284 W370 F396
BS04 H4B B S104 R367 A448 W449 S36 R288 A369 W370
BS05 Q16 B V106 P336 V338 F355 W358 E363 V38 P257 V259 F276 W279 E284 BindingDB: Ki=6727nM
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:4cx0, PDBe:4cx0, PDBj:4cx0
PDBsum4cx0
PubMed25089924
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

[Back to BioLiP]