4FNC: G/T mismatch-specific thymine DNA glycosylase

Human TDG in a post-reactive complex with 5-hydroxymethyluracil (5hmU). Determined by X-ray diffraction at 2.49 Å resolution. Released 19 Sept 2012.

Method: X-ray diffraction
Resolution: 2.49 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,714
Mol. weight: 40.64 kDa
Ligands: HMU
Released: 19 Sept 2012

Explore 4FNC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4FNC contains 10 α-helices and 8 β-strands across 1 chain. 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	111	1	1
β-strand	114	1	1
α-helix	116-121	6
β-strand	127	1	2
β-strand	134-138	5	2
α-helix	143-148	6
α-helix	159-165	7
α-helix	175-180	6
α-helix	181-184	4
β-strand	187-191	5	2
α-helix	200-202	3
α-helix	205-222	18
β-strand	226-230	5	2
α-helix	232-242	11
β-strand	253-254	2	2
α-helix	258-259	2
β-strand	265-269	5	2
α-helix	282-304	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G/T mismatch-specific thymine DNA glycosylase	A	protein	204	Homo sapiens	Q13569 (AlphaFold model)
DNA (28-mer)	C	DNA	28
DNA (29-mer)	D	DNA	29

Sequence of entity 1 (A), FASTA

>4FNC_1 G/T mismatch-specific thymine DNA glycosylase (chains A)
GSHMASFNGVSEAELLTKTLPDILTFNLDIVIIGINPGLMAAYKGHHYPGPGNHFWKCLF
MSGLSEVQLNHMDDHTLPGKYGIGFTNMVERTTPGSKDLSSKEFREGGRILVQKLQKYQP
RIAVFNGKCIYEIFSKEVFGVKVKNLEFGLQPHKIPDTETLCYVMPSSSARCAQFPRAQD
KVHYYIKLKDLRDQLKGIERNMDV

Sequence of entity 2 (C), FASTA

>4FNC_2 DNA (28-MER) (chains C)
CAGCTCTGTACGTGAGCAGTGGACAGCT

Sequence of entity 3 (D), FASTA

>4FNC_3 DNA (29-MER) (chains D)
AGCTGTCCACTGCTCAXGTACAGAGCTGT

Ligands and cofactors

ID	Name	Formula	Copies
HMU	5-hydroxymethyl uracil	C5 H6 N2 O3	1

Primary citation

Excision of 5-hydroxymethyluracil and 5-carboxylcytosine by the thymine DNA glycosylase domain: its structural basis and implications for active DNA demethylation. Hashimoto, H., Hong, S., Bhagwat, A.S. et al. Nucleic Acids Res (2012) 40:10203-10214. DOI 10.1093/nar/gks845 · PubMed

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

4Z47 1.45 Å, Structure of the enzyme-product complex resulting from TDG action on a GU mismatch in…
5HF7 1.54 Å, TDG enzyme-substrate complex
6U17 1.55 Å, Human thymine DNA glycosylase bound to DNA with 2'-F-5-carboxyl-dC substrate analog
6U16 1.6 Å, Human thymine DNA glycosylase N140A mutant bound to DNA with 5-carboxyl-dC substrate
5FF8 1.7 Å, TDG enzyme-product complex
5JXY 1.71 Å, Enzyme-substrate complex of TDG catalytic domain bound to a G/U analog
4XEG 1.72 Å, Structure of the enzyme-product complex resulting from TDG action on a G/hmU mismatch
4Z3A 1.72 Å, Acetate-free structure of the enzyme-product complex resulting from TDG action on a GU…
4Z7Z 1.83 Å, Structure of the enzyme-product complex resulting from TDG action on a GT mismatch in…
4Z7B 2.02 Å, Structure of the enzyme-product complex resulting from TDG action on a GfC mismatch
1WYW 2.1 Å, Crystal Structure of SUMO1-conjugated thymine DNA glycosylase
2D07 2.1 Å, Crystal Structure of SUMO-3-modified Thymine-DNA Glycosylase

Browse structure collections

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