Structure of PDB 5vsm Chain A Binding Site BS01
Receptor Information
>5vsm Chain A (length=258) Species:
10090
(Mus musculus) [
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VSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLEKINF
SGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKDYGEY
LDILAISCDSFDEQVNALIGRGQGKKNHVENLQKLRRWCRDYKVAFKINS
VINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGEDALREAERFLIS
NEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTDPSKSILD
VGVEEAIK
Ligand information
Ligand ID
SF4
InChI
InChI=1S/4Fe.4S
InChIKey
LJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 2.0.7
[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385
S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
Formula
Fe4 S4
Name
IRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain
5vsm Chain A Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
5vsm
Structural studies of viperin, an antiviral radical SAM enzyme.
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
C84 Y86 C88 C91 G126 N158 R194
Binding residue
(residue number reindexed from 1)
C11 Y13 C15 C18 G53 N85 R121
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
C84 C88 C91
Catalytic site (residue number reindexed from 1)
C11 C15 C18
Enzyme Commision number
4.2.-.-
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
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:5vsm
,
PDBe:5vsm
,
PDBj:5vsm
PDBsum
5vsm
PubMed
28607080
UniProt
Q8CBB9
|RSAD2_MOUSE S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 (Gene Name=Rsad2)
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