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1LQJ

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016787molecular_functionhydrolase activity
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
A0097510biological_processbase-excision repair, AP site formation via deaminated base removal
B0004844molecular_functionuracil DNA N-glycosylase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0097510biological_processbase-excision repair, AP site formation via deaminated base removal
C0004844molecular_functionuracil DNA N-glycosylase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0097510biological_processbase-excision repair, AP site formation via deaminated base removal
D0004844molecular_functionuracil DNA N-glycosylase activity
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006281biological_processDNA repair
D0006284biological_processbase-excision repair
D0016787molecular_functionhydrolase activity
D0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
D0097510biological_processbase-excision repair, AP site formation via deaminated base removal
Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS57-TYR66

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
APRO65
BPRO65
CPRO65
DPRO65

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AHIS187
AASP64

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
BHIS187
BASP64

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
CHIS187
CASP64

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
DHIS187
DASP64

site_idMCSA1
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
APRO65activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
AHIS67activator, steric role
ASER78activator, steric role
APRO188covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
BPRO65activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
BHIS67activator, steric role
BSER78activator, steric role
BPRO188covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA3
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
CPRO65activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
CHIS67activator, steric role
CSER78activator, steric role
CPRO188covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA4
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
DPRO65activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
DHIS67activator, steric role
DSER78activator, steric role
DPRO188covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2024-07-24

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