Structure of PDB 4cwx Chain B

Receptor sequence
>4cwxB (length=402) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPPAEQLLSQAR
DFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAKQAW
RNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLRSAI
TVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCIQHG
WTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAALGL
RWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNILED
VAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATVSFM
KHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRYQPD
PW
3D structure
PDB4cwx Mobility of a Conserved Tyrosine Residue Controls Isoform-Dependent Enzyme-Inhibitor Interactions in Nitric Oxide Synthases.
ChainB
Resolution2.15 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) C106 R109 W278 E283
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 Q464 E465 W367 F382 Q384 E385
BS02 HEM B W180 C186 V187 M341 F355 W358 E363 W449 F475 Y477 W100 C106 V107 M261 F275 W278 E283 W369 F395 Y397
BS03 H4B B S104 R367 A448 W449 S36 R287 A368 W369
BS04 HW0 B L107 P336 V338 E363 W449 Y477 L39 P256 V258 E283 W369 Y397 MOAD: Ki=33.5uM
BS05 ZN B C96 C101 C28 C33
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:4cwx, PDBe:4cwx, PDBj:4cwx
PDBsum4cwx
PubMed25089924
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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