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1AKZ

HUMAN URACIL-DNA GLYCOSYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS138-TYR147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP
ChainResidueDetails
AHIS154

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP, ECO:0000312|PDB:4SKN
ChainResidueDetails
AALA153
APRO167
AGLN213
AGLY277

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000312|PDB:4SKN
ChainResidueDetails
ACYS157
ASER178
AILE256
APHE279
AARG282
ASER285

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Essential for UNG2 recruitment to nuclear foci => ECO:0000269|PubMed:22521144
ChainResidueDetails
ASER88

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
AGLY295

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP145
AHIS268

237423

PDB entries from 2025-06-11

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