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1LMZ

Solution Structure of 3-Methyladenine DNA Glycosylase I (TAG)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005515molecular_functionprotein binding
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006307biological_processDNA alkylation repair
A0006974biological_processDNA damage response
A0008725molecular_functionDNA-3-methyladenine glycosylase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12654914","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"13129925","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1NKU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1P7M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1p7m
ChainResidueDetails
AGLU38
ATRP46
ATYR16

site_idMCSA1
Number of Residues3
DetailsM-CSA 655
ChainResidueDetails
ATYR16electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AGLU38electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ATRP46electrostatic stabiliser, van der waals interaction

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PDB entries from 2025-08-06

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