Structure of PDB 3w1k Chain C Binding Site BS02
Receptor Information
>3w1k Chain C (length=452) Species:
224324
(Aquifex aeolicus VF5) [
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MKSLLRQIPQISKVVEIFAKAYPEIYVVKAAREVAEKYRKEIIEGARADL
NGFLEDVERKIKSLMKPNIKRVINATGVVINTNLGRAPLSKDVINFISEI
ANGYSNLEYNLEEGKRGSRIAHIEKYLNELTGAESSFVVNNNAGAVFLVL
NTLAEGKEVIISRGELVEIGGSFRIPDIMKKSGAILREVGTTNKTKVSDY
EGAINQNTALLMKVHKSNFYMEGFVEEVKLEDLVKLGHKYGIPTYYDAGS
GLLINLKEFGISVDEPNFRDCISLGIDLVSGSGDKLLGGPQAGIIVGKKN
LIEKIKKNPIARALRIDKLTLSGLEMTLKLYFEKRYEDIPVIRMLTQDEK
ALRQKAKRLEKLLKDIPGLKISVIKDKAKPGGGSLPELELPTYCVAIRHD
RLSSQELSRRLRLAEPPIVCRIREDQLLFDMRTVFHEDLKTIKKTLQELL
SI
Ligand information
>3w1k Chain H (length=92) [
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gggaguagauaggcgcuggugugccuccuagacuucaaaucuacggucuc
gcuauuuaagcgagagguggguucgauucccacauacucccg
<<<<<<<...<<<<<......>>>>><<<<<<.......>>>>.>><<<<
<<<.....>>>>>>>.<<<<<.......>>>>>.>>>>>>>.
Receptor-Ligand Complex Structure
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PDB
3w1k
Decameric SelA-tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation
Resolution
7.5 Å
Binding residue
(original residue number in PDB)
K257 S262
Binding residue
(residue number reindexed from 1)
K257 S262
Binding affinity
PDBbind-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
PDBsum
3w1k
PubMed
23559248
UniProt
O67140
|SELA_AQUAE L-seryl-tRNA(Sec) selenium transferase (Gene Name=selA)
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