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3EUG

CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED

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 Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 230
ChainResidue
AGLN63
AASP64
AALA76
APHE77
AASN123
AHIS187
AHOH309
AHOH384

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 231
ChainResidue
ALYS15
APHE45
APHE48
AGLN212
AHIS213
AHOH397
AHOH454
AHOH529
AHOH565

site_idURA
Number of Residues1
DetailsURACIL BINDING SITE
ChainResidue
AASP64

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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AASP64

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

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

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PDB entries from 2025-06-25

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