Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3FCI

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 Residues19
DetailsBINDING SITE FOR RESIDUE 3FI A 1
ChainResidue
AHOH75
AGLY246
ASER247
ATYR248
AHIS268
ASER273
ALYS293
AHOH497
AHOH598
AHOH648
AHOH704
AHOH79
AGLY143
AGLN144
AASP145
ATYR147
ACYS157
APHE158
AASN204

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 305
ChainResidue
AGLU111
ALYS114
AHOH513
AHOH583

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SCN A 2
ChainResidue
AVAL109
AARG113
AHOH563

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN A 3
ChainResidue
APRO100
ATYR101
AGLN224
ALYS297
AHOH494
AHOH561

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

226707

PDB entries from 2024-10-30

PDB statisticsPDBj update infoContact PDBjnumon