3UFJ: Human Thymine DNA Glycosylase

Human Thymine DNA Glycosylase Bound to Substrate Analog 2'-fluoro-2'-deoxyuridine. Determined by X-ray diffraction at 2.97 Å resolution. Released 25 Apr 2012.

Method
X-ray diffraction
Resolution
2.97 Å
Organism
Homo sapiens
Chains
6
Atoms
4,509
Mol. weight
74.43 kDa
Released
25 Apr 2012

Explore 3UFJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UFJ contains 19 α-helices and 12 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 10 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix124-1263
β-strand134-13851
α-helix143-1486
β-strand15712
α-helix159-1668
α-helix175-1806
α-helix181-1855
β-strand187-19151
α-helix205-22218
β-strand226-23051
α-helix232-2387
α-helix239-2435
β-strand253-25531
α-helix258-2592
β-strand265-26951
β-strand27312
α-helix287-30115
Chain B: 9 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand134-13853
α-helix143-1486
α-helix159-1635
α-helix164-1685
α-helix175-1806
α-helix181-1855
β-strand187-19153
α-helix206-22217
β-strand226-23053
α-helix232-2387
α-helix239-2435
β-strand253-25863
β-strand265-26953
α-helix287-30115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
G/T mismatch-specific thymine DNA glycosylaseA, Bprotein204Homo sapiensQ13569 (AlphaFold model)
5'-d(*cp*ap*gp*cp*tp*cp*tp*gp*tp*ap*cp*gp*tp*gp*ap*gp*cp*ap*gp*tp*gp*gp*a)-3'C, EDNA23
5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(UF2)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3'D, FDNA23
Sequence of entity 1 (A, B), FASTA
>3UFJ_1 G/T mismatch-specific thymine DNA glycosylase (chains A, B)
GSHMASFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLF
MSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQP
RIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQD
KVHYYIKLKDLRDQLKGIERNMDV
Sequence of entity 2 (C, E), FASTA
>3UFJ_2 5'-D(*CP*AP*GP*CP*TP*CP*TP*GP*TP*AP*CP*GP*TP*GP*AP*GP*CP*AP*GP*TP*GP*GP*A)-3' (chains C, E)
CAGCTCTGTACGTGAGCAGTGGA
Sequence of entity 3 (D, F), FASTA
>3UFJ_3 5'-D(*CP*CP*AP*CP*TP*GP*CP*TP*CP*AP*(UF2)P*GP*TP*AP*CP*AP*GP*AP*GP*CP*TP*GP*T)-3' (chains D, F)
CCACTGCTCAXGTACAGAGCTGT

Primary citation

Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA. Maiti, A., Noon, M.S., Mackerell, A.D. et al. Proc Natl Acad Sci U S A (2012) 109:8091-8096. DOI 10.1073/pnas.1201010109 · PubMed

Other PDB entries of the same protein (UniProt Q13569 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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