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4B24

Unprecedented sculpting of DNA at abasic sites by DNA glycosylase homolog Mag2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000725biological_processrecombinational repair
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0003905molecular_functionalkylbase DNA N-glycosylase activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006285biological_processbase-excision repair, AP site formation
A0006289biological_processnucleotide-excision repair
A0006307biological_processDNA alkylation repair
A0006974biological_processDNA damage response
A0032131molecular_functionalkylated DNA binding
A0032993cellular_componentprotein-DNA complex
A0140431molecular_functionDNA-(abasic site) binding
Functional Information from PROSITE/UniProt
site_idPS00516
Number of Residues25
DetailsALKYLBASE_DNA_GLYCOS Alkylbase DNA glycosidases alkA family signature. GVKrWTIeMYsIftlgrldiMpaDD
ChainResidueDetails
AGLY138-ASP162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:23245849, ECO:0000269|PubMed:23273506
ChainResidueDetails
ALYS53
AHIS91
ALYS97
ALYS137
AGLY138
ALYS140
ATHR143
ASER163

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:23273506
ChainResidueDetails
ALEU54
ASER61
AGLY94
ASER96
ALYS99
AGLU102

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23245849
ChainResidueDetails
ATHR164

218853

PDB entries from 2024-04-24

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