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6LYJ

The crystal structure of SAUGI/EBVUDG complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0042025cellular_componenthost cell nucleus
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
B0004844molecular_functionuracil DNA N-glycosylase activity
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0042025cellular_componenthost cell nucleus
B0097510biological_processbase-excision repair, AP site formation via deaminated base removal
C0046872molecular_functionmetal ion binding
D0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS84-TYR93

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04046
ChainResidueDetails
AASP91
BASP91

226707

PDB entries from 2024-10-30

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