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1EUI

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006974biological_processDNA damage response
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
B0006974biological_processDNA damage response
B0016787molecular_functionhydrolase activity
B0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0097510biological_processbase-excision repair, AP site formation via deaminated base removal
C0005515molecular_functionprotein binding
D0005515molecular_functionprotein binding
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 Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
APRO65
BPRO65

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_idMCSA1
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
AASP64activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
ATYR66activator, steric role
APHE77activator, steric role
AHIS187covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 71
ChainResidueDetails
BASP64activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
BTYR66activator, steric role
BPHE77activator, steric role
BHIS187covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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PDB entries from 2025-07-02

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