Structure of PDB 3w1k Chain C Binding Site BS02

Receptor Information
>3w1k Chain C (length=452) Species: 224324 (Aquifex aeolicus VF5) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKSLLRQIPQISKVVEIFAKAYPEIYVVKAAREVAEKYRKEIIEGARADL
NGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEI
ANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVL
NTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDY
EGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGS
GLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKN
LIEKIKKNPIARALRIDKLTLSGLEMTLKLYFEKRYEDIPVIRMLTQDEK
ALRQKAKRLEKLLKDIPGLKISVIKDKAKPGGGSLPELELPTYCVAIRHD
RLSSQELSRRLRLAEPPIVCRIREDQLLFDMRTVFHEDLKTIKKTLQELL
SI
Ligand information
>3w1k Chain H (length=92) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
gggaguagauaggcgcuggugugccuccuagacuucaaaucuacggucuc
gcuauuuaagcgagagguggguucgauucccacauacucccg
<<<<<<<...<<<<<......>>>>><<<<<<.......>>>>.>><<<<
<<<.....>>>>>>>.<<<<<.......>>>>>.>>>>>>>.
Receptor-Ligand Complex Structure
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PDB3w1k Decameric SelA-tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation
Resolution7.5 Å
Binding residue
(original residue number in PDB)
K257 S262
Binding residue
(residue number reindexed from 1)
K257 S262
Binding affinityPDBbind-CN: Kd=75nM
Enzymatic activity
Enzyme Commision number 2.9.1.1: L-seryl-tRNA(Sec) selenium transferase.
Gene Ontology
Molecular Function
GO:0004125 L-seryl-tRNA(Sec) selenium transferase activity
GO:0016740 transferase activity
GO:0042802 identical protein binding
Biological Process
GO:0001514 selenocysteine incorporation
GO:0006412 translation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3w1k, PDBe:3w1k, PDBj:3w1k
PDBsum3w1k
PubMed23559248
UniProtO67140|SELA_AQUAE L-seryl-tRNA(Sec) selenium transferase (Gene Name=selA)

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