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3TKB

crystal structure of human uracil-DNA glycosylase D183G/K302R mutant

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
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD A 4496
ChainResidue
AGLY280
AARG282
ALYS286

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE IMD A 305
ChainResidue
AHOH29
ALYS175
APHE279

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 Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP
ChainResidueDetails
AASP145

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000269|PubMed:9724657, ECO:0000312|PDB:1SSP, ECO:0000312|PDB:4SKN
ChainResidueDetails
AGLN144
APHE158
AASN204
AHIS268

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:8900285, ECO:0000312|PDB:4SKN
ChainResidueDetails
AHIS148
ASER169
ASER247
ASER270
ASER273
AARG276

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS286

236963

PDB entries from 2025-06-04

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