2.1.1.217: tRNA (adenine22-N1)-methyltransferase
This is an abbreviated version!
For detailed information about tRNA (adenine22-N1)-methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.217
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2.1.1.217
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mtases
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methyltransferases
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adomet
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rna-binding
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groove
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sam-dependent
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class-i
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ligand-free
- 2.1.1.217
- mtases
- methyltransferases
- adomet
-
rna-binding
-
groove
-
sam-dependent
-
class-i
-
ligand-free
Reaction
Synonyms
BsTrmK, Class I MTase, EC 2.1.1.36, m1A22 MTase, m1A22 tRNA methyltransferase, Sp1610, TrmK, tRNA: m1A22 methyltransferase, yqfN
ECTree
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Cofactor
Cofactor on EC 2.1.1.217 - tRNA (adenine22-N1)-methyltransferase
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S-adenosyl-L-methionine
SAM, enzyme binding structure analysis, overview. SAM is modelled into the active site of BsTrmK, guided by the crystal structure of SAM-bound TrmK from Streptomyces pneumoniae (PDB ID 3KU1). The SAM cofactor is bound at the centre of the catalytic domain in a pocket with residues harbouring negative electrostatic potentials conserved amongst COG2384 proteins. The methyl group is pointing towards a region of positively charged and well conserved residues, likely important for tRNA binding