Structure of PDB 5vsl Chain A

Receptor sequence
>5vslA (length=262) Species: 10090 (Mus musculus) [Search protein sequence]
TPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKI
NFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYG
EYLDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKI
NSVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFL
ISNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTDPSKSI
LDVGVEEAIKFS
3D structure
PDB5vsl Structural studies of viperin, an antiviral radical SAM enzyme.
ChainA
Resolution1.972 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) C84 C88 C91
Catalytic site (residue number reindexed from 1) C13 C17 C20
Enzyme Commision number 4.2.-.-
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 SF4 A C84 Y86 C88 C91 G126 N158 R194 C13 Y15 C17 C20 G55 N87 R123
BS02 SAH A F90 F92 S124 G125 G126 E127 V156 S157 N158 S180 R194 N222 V224 C251 L252 F19 F21 S53 G54 G55 E56 V85 S86 N87 S109 R123 N151 V153 C180 L181
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0051536 iron-sulfur cluster binding
Biological Process
GO:0051607 defense response to virus
Cellular Component
GO:0005789 endoplasmic reticulum membrane
GO:0005811 lipid droplet

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5vsl, PDBe:5vsl, PDBj:5vsl
PDBsum5vsl
PubMed28607080
UniProtQ8CBB9|RSAD2_MOUSE S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 (Gene Name=Rsad2)

[Back to BioLiP]