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5AYR

The crystal structure of SAUGI/human UDG complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004844molecular_functionuracil DNA N-glycosylase activity
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
B0046872molecular_functionmetal ion binding
C0004844molecular_functionuracil DNA N-glycosylase activity
C0006281biological_processDNA repair
C0006284biological_processbase-excision repair
C0016799molecular_functionhydrolase activity, hydrolyzing N-glycosyl compounds
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MG A 900
ChainResidue
AASP145
AASN215
AHOH1006
AHOH1009
AHOH1071
BHOH1008

site_idAC2
Number of Residues6
Detailsbinding site for residue MG B 900
ChainResidue
BHOH1027
DASP88
DMG900
BASP88
BMET89
BHOH1015

site_idAC3
Number of Residues6
Detailsbinding site for residue MG C 900
ChainResidue
CASP145
CASN215
CHOH1007
CHOH1009
CHOH1029
CHOH1071

site_idAC4
Number of Residues6
Detailsbinding site for residue MG D 900
ChainResidue
BASP88
BMG900
BHOH1015
DASP88
DMET89
DHOH1007

Functional Information from PROSITE/UniProt
site_idPS00130
Number of Residues10
DetailsU_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY
ChainResidueDetails
ALYS138-TYR147

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03166
ChainResidueDetails
AASP145
CASP145

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS286
CLYS286

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PDB entries from 2024-10-09

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