Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1UUG

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE:INHIBITOR COMPLEX WITH WILD-TYPE UDG AND WILD-TYPE UGI

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
B0005515molecular_functionprotein binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0006974biological_processDNA damage response
C0016787molecular_functionhydrolase activity
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
C0097510biological_processbase-excision repair, AP site formation via deaminated base removal
D0005515molecular_functionprotein binding
Functional Information from PDB Data
site_idGB1
Number of Residues1
DetailsGENERAL BASE TO ACTIVATE NUCLEOPHILIC WATER
ChainResidue
AASP64

site_idGB2
Number of Residues1
DetailsGENERAL BASE TO ACTIVATE NUCLEOPHILIC WATER
ChainResidue
CASP64

site_idUR1
Number of Residues5
DetailsURACIL BINDING RESIDUES BY HOMOLOGY
ChainResidue
AGLN63
ATYR66
APHE77
AASN123
AHIS187

site_idUR2
Number of Residues5
DetailsURACIL BINDING RESIDUES BY HOMOLOGY
ChainResidue
CASN123
CHIS187
CGLN63
CTYR66
CPHE77

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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

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
CHIS187
CASP64

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
CASP64activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
CTYR66activator, steric role
CPHE77activator, steric role
CHIS187covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon