Structure of PDB 2adm Chain A

Receptor sequence
>2admA (length=385) Species: 271 (Thermus aquaticus) [Search protein sequence]
VETPPEVVDFMVSLAEAPRGGRVLEPACAHGPFLRAFREAHGTGYRFVGV
EIDPKALDLPPWAEGILADFLLWEPGEAFDLILGNPPYGIVGVFKAVKDL
YKKAFSTWKGKYNLYGAFLEKAVRLLKPGGVLVFVVPATWLVLEDFALLR
EFLAREGKTSVYYLGEVFPQKKVSAVVIRFQKSGKGLSLWDTQESESGFT
PILWAEYPHWEGEIIRFETEETRKLEISGMPLGDLFHIRFAARSPEFKKH
PAVRKEPGPGLVPVLTGRNLKPGWVDYEKNHSGLWMPKERAKELRDFYAT
PHLVVAHTKGTRVVAAWDERAYPWREEFHLLPKEGVRLDPSTLVQWLNSE
AMQKHVRTLYRDFVPHLTLRMLERLPVRREYGFHT
3D structure
PDB2adm 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
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N105 P106 Y108 F196
Catalytic site (residue number reindexed from 1) N85 P86 Y88 F168
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 SAM A A47 C48 P52 E71 I72 D89 F90 N105 P107 A27 C28 P32 E51 I52 D69 F70 N85 P87
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:2adm, PDBe:2adm, PDBj:2adm
PDBsum2adm
PubMed8995524
UniProtP14385|MTTA_THEAQ Type II methyltransferase M.TaqI (Gene Name=taqIM)

[Back to BioLiP]