Structure of PDB 1aqj Chain A

Receptor sequence
>1aqjA (length=381) Species: 271 (Thermus aquaticus) [Search protein sequence]
VETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREAHGTGYRFVGV
EIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVAVKDLYKKA
FSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLREFLA
REGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFTPILW
AEYPHWEGEIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKHPAVR
KEPGPGLVPVLTGRNLKPGWVDYEKNHSGLWMPKERAKELRDFYATPHLV
VAHTKGTRVVAAWDERAYPWREEFHLLPKEGVRLDPSSLVQWLNSEAMQK
HVRTLYRDFVPHLTLRMLERLPVRREYGFHT
3D structure
PDB1aqj Differential binding of S-adenosylmethionine S-adenosylhomocysteine and Sinefungin to the adenine-specific DNA methyltransferase M.TaqI.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N105 P106 Y108 F196
Catalytic site (residue number reindexed from 1) N85 P86 Y88 F164
Enzyme Commision number 2.1.1.72: site-specific DNA-methyltransferase (adenine-specific).
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 SFG A V21 A47 E71 F90 N105 P106 P107 Y108 F146 V1 A27 E51 F70 N85 P86 P87 Y88 F114 PDBbind-CN: -logKd/Ki=6.47,Kd=0.34uM
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0008168 methyltransferase activity
GO:0009007 site-specific DNA-methyltransferase (adenine-specific) activity
Biological Process
GO:0006304 DNA modification
GO:0009307 DNA restriction-modification system
GO:0032259 methylation

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1aqj, PDBe:1aqj, PDBj:1aqj
PDBsum1aqj
PubMed8995524
UniProtP14385|MTTA_THEAQ Type II methyltransferase M.TaqI (Gene Name=taqIM)

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