Structure of PDB 6q2q Chain B Binding Site BS01

Receptor Information
>6q2q Chain B (length=290) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
RTTPVSVNYHFTRQCNYKCGFCFHTAKTSFVLPLEEAKRGLLLLKQAGLE
KINFSGGEPFLQDRGEYLGKLVRFCKEELALPSVSIVSNGSLIRERWFKD
YGEYLDILAISCDSFDEQVNALIGRGQNHVENLQKLRRWCRDYKVAFKIN
SVINRFNVDEDMNEHIKALSPVRWKVFQCLLIEGENSGADALRAAERFLI
SNEEFETFLERHKEVSCLVPESNQKMKDSYLILDEYMRFLNCTGGRKDPS
KSILDVGVEEAIKFSGFDEKMFLKRGGKYVWSKADLKLDW
Ligand information
Ligand IDSF4
InChIInChI=1S/4Fe.4S
InChIKeyLJBDFODJNLIPKO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7[S]12[Fe]3[S]4[Fe]1[S]5[Fe]2[S]3[Fe]45
CACTVS 3.385S1[Fe]S[Fe]1.S2[Fe]S[Fe]2
FormulaFe4 S4
NameIRON/SULFUR CLUSTER
ChEMBL
DrugBank
ZINC
PDB chain6q2q Chain B Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6q2q Structural Basis of the Substrate Selectivity of Viperin.
Resolution1.892 Å
Binding residue
(original residue number in PDB)		C84 Y86 C88 C91 G126 N158 R194
Binding residue
(residue number reindexed from 1)		C15 Y17 C19 C22 G57 N89 R125
Annotation score1
Enzymatic activity
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:6q2q, PDBe:6q2q, PDBj:6q2q
PDBsum6q2q
PubMed31917549
UniProtQ8CBB9|RSAD2_MOUSE S-adenosylmethionine-dependent nucleotide dehydratase RSAD2 (Gene Name=Rsad2)

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