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1NKU

NMR Solution Structure of Zinc-binding protein 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
A0008725molecular_functionDNA-3-methyladenine glycosylase activity
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 188
ChainResidue
ACYS4
AHIS17
ATRP21
AHIS175
ACYS179

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12654914, ECO:0000269|PubMed:13129925, ECO:0007744|PDB:1NKU, ECO:0007744|PDB:1P7M
ChainResidueDetails
ACYS4
AHIS17
AHIS175
ACYS179

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 2024-07-17

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