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3FCF

Complex of UNG2 and a fragment-based designed inhibitor

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 Residues20
DetailsBINDING SITE FOR RESIDUE FCF A 1
ChainResidue
ASCN2
AASN204
AGLY246
ASER247
ATYR248
AHIS268
ASER270
ASER273
AHOH306
AHOH364
AHOH384
AHOH40
AHOH398
AGLY143
AGLN144
AASP145
ATYR147
ACYS157
APHE158
ASER169

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SCN A 305
ChainResidue
AHOH44
AMET106
AVAL109
AARG113

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SCN A 2
ChainResidue
AFCF1
ATYR147
AHIS148
AGLY149
AGLN152

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
ChainResidueDetails
AASP145

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS286

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eug
ChainResidueDetails
AASP145
AHIS268

219140

PDB entries from 2024-05-01

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