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6LYV

The crystal structure of SAUGI/KSHVUDG 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
B0046872molecular_functionmetal ion binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0042025cellular_componenthost cell nucleus
C0097510biological_processbase-excision repair, AP site formation via deaminated base removal
D0046872molecular_functionmetal ion binding
E0004844molecular_functionuracil DNA N-glycosylase activity
E0006281biological_processDNA repair
E0006284biological_processbase-excision repair
E0016787molecular_functionhydrolase activity
E0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
E0042025cellular_componenthost cell nucleus
E0097510biological_processbase-excision repair, AP site formation via deaminated base removal
F0046872molecular_functionmetal ion binding
G0004844molecular_functionuracil DNA N-glycosylase activity
G0006281biological_processDNA repair
G0006284biological_processbase-excision repair
G0016787molecular_functionhydrolase activity
G0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
G0042025cellular_componenthost cell nucleus
G0097510biological_processbase-excision repair, AP site formation via deaminated base removal
H0046872molecular_functionmetal ion binding
I0004844molecular_functionuracil DNA N-glycosylase activity
I0006281biological_processDNA repair
I0006284biological_processbase-excision repair
I0016787molecular_functionhydrolase activity
I0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
I0042025cellular_componenthost cell nucleus
I0097510biological_processbase-excision repair, AP site formation via deaminated base removal
J0046872molecular_functionmetal ion binding
K0004844molecular_functionuracil DNA N-glycosylase activity
K0006281biological_processDNA repair
K0006284biological_processbase-excision repair
K0016787molecular_functionhydrolase activity
K0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
K0042025cellular_componenthost cell nucleus
K0097510biological_processbase-excision repair, AP site formation via deaminated base removal
L0046872molecular_functionmetal ion binding
M0004844molecular_functionuracil DNA N-glycosylase activity
M0006281biological_processDNA repair
M0006284biological_processbase-excision repair
M0016787molecular_functionhydrolase activity
M0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
M0042025cellular_componenthost cell nucleus
M0097510biological_processbase-excision repair, AP site formation via deaminated base removal
N0046872molecular_functionmetal ion binding
O0004844molecular_functionuracil DNA N-glycosylase activity
O0006281biological_processDNA repair
O0006284biological_processbase-excision repair
O0016787molecular_functionhydrolase activity
O0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
O0042025cellular_componenthost cell nucleus
O0097510biological_processbase-excision repair, AP site formation via deaminated base removal
P0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS64-TYR73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_04046
ChainResidueDetails
AASP71
CASP71
EASP71
GASP71
IASP71
KASP71
MASP71
OASP71

224004

PDB entries from 2024-08-21

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