Structure of PDB 3ubt Chain A

Receptor sequence
>3ubtA (length=328) Species: 197575 (Haemophilus aegyptius) [Search protein sequence]
MNLISLFSGAGGLDLGFQKAGFRIICANEYDKSIWKTYESNHSAKLIKGD
ISKISSDEFPKCDGIIGGPPSQSWSEGGSLRGIDDPRGKLFYEYIRILKQ
KKPIFFLAENVKGMMAQRHNKAVQEFIQEFDNAGYDVHIILLNANDYGVA
QDRKRVFYIGFRKELNINYLPPIPHLIKPTFKDVIWDLKDNPIPALDKNK
TNGNKCIYPNHEYFIGSYSTIFMSRNRVRQWNEPAFTVQASGRQCQLHPQ
APVMLKVSKNLNKFVEGKEHLYRRLTVRECARVQGFPDDFIFHYESLNDG
YKMIGNAVPVNLAYEIAKTIKSALEICK
3D structure
PDB3ubt Structural origins of DNA target selection and nucleobase extrusion by a DNA Cytosine methyltransferase.
ChainA
Resolution2.502 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S71 E109 R153 R155
Catalytic site (residue number reindexed from 1) S71 E109 R153 R155
Enzyme Commision number 2.1.1.37: DNA (cytosine-5-)-methyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 dna A S219 T220 I221 R225 R243 S219 T220 I221 R225 R243
BS02 dna A R225 R227 F236 T237 Q239 R225 R227 F236 T237 Q239
BS03 ATP A Y30 D50 I51 L90 N306 Y30 D50 I51 L90 N306
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003886 DNA (cytosine-5-)-methyltransferase activity
GO:0005524 ATP binding
GO:0008168 methyltransferase activity
Biological Process
GO:0009307 DNA restriction-modification system
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3ubt, PDBe:3ubt, PDBj:3ubt
PDBsum3ubt
PubMed23012373
UniProtP20589|MTH3_HAEAE Type II methyltransferase M.HaeIII (Gene Name=haeIIIM)

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