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3UF7

Co-crystal structure of Escherichia coli uracil-DNA glycosylase and a C-terminal fragement of the single-stranded DNA-binding 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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 238
ChainResidue
ALYS57
AGLU215
ATHR216

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 239
ChainResidue
ALYS94
AARG105
AHOH364
AHOH428
AHOH472
AHOH527

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 A 240
ChainResidue
AARG49
AARG116

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 241
ChainResidue
AASN3
AHIS155
AARG156
AGLU157
AHOH510

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 Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

Catalytic Information from CSA
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

247536

PDB entries from 2026-01-14

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