Structure of PDB 4cum Chain B

Receptor sequence
>4cumB (length=405) Species: 9913 (Bos taurus) [Search protein sequence]
KFPRVKNWELGSITYDTLCAQSQQDGPCTPRRCLGSLVLPRKLPAEQLLS
QARDFINQYYSSIKRSGSQAHEERLQEVEAEVASTGTYHLRESELVFGAK
QAWRNAPRCVGRIQWGKLQVFDARDCSSAQEMFTYICNHIKYATNRGNLR
SAITVFPQRAPGRGDFRIWNSQLVRYAGYRQQDGSVRGDPANVEITELCI
QHGWTPGNGRFDVLPLLLQAPDEAPELFVLPPELVLEVPLEHPTLEWFAA
LGLRWYALPAVSNMLLEIGGLEFSAAPFSGWYMSTEIGTRNLCDPHRYNI
LEDVAVCMDLDTRTTSSLWKDKAAVEINLAVLHSFQLAKVTIVDHHAATV
SFMKHLDNEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYILSPAFRY
QPDPW
3D structure
PDB4cum Communication between the Zinc and Tetrahydrobiopterin Binding Sites in Nitric Oxide Synthase.
ChainB
Resolution2.33 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 WS7 B W447 F462 W370 F385
BS02 ZN B C96 C101 C28 C33
BS03 ARG B Q249 Y359 E363 N368 Q172 Y282 E286 N291
BS04 HEM B W180 C186 V187 M341 F355 G357 W358 E363 W449 F475 Y477 W103 C109 V110 M264 F278 G280 W281 E286 W372 F398 Y400
BS05 WS7 B S104 R367 A448 W449 S36 R290 A371 W372
Gene Ontology
Molecular Function
GO:0004517 nitric-oxide synthase activity
Biological Process
GO:0006809 nitric oxide biosynthetic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4cum, PDBe:4cum, PDBj:4cum
PDBsum4cum
PubMed24819538
UniProtP29473|NOS3_BOVIN Nitric oxide synthase 3 (Gene Name=NOS3)

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