1SSP: Wild-type uracil-DNA glycosylase

Wild-type uracil-DNA glycosylase bound to uracil-containing DNA. Determined by X-ray diffraction at 1.9 Å resolution. Released 6 May 1999.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,498
Mol. weight: 31.95 kDa
Ligands: URA
Released: 6 May 1999

Explore 1SSP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SSP contains 14 α-helices and 7 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 E: 14 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	87-93	7
α-helix	94-96	3
α-helix	100-115	16
β-strand	118-119	2	1
α-helix	122-124	3
α-helix	127-129	3
α-helix	134-136	3
β-strand	139-143	5	2
α-helix	165-167	3
α-helix	168-180	13
α-helix	193-197	5
β-strand	200-204	5	2
β-strand	209-210	2	1
β-strand	213	1	1
α-helix	222-236	15
β-strand	241-245	5	2
α-helix	249-255	7
β-strand	262-266	5	2
α-helix	274-276	3
α-helix	283-293	11
α-helix	297-299	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
5'-D(CPTPGPTP(D1P)PAPTPCPTPT)-3'	A	DNA	10
5'-d(apapapgpaptpapapcpap*g)-3'	B	DNA	11
Uracil-DNA glycosylase	E	protein	223	Homo sapiens	P13051 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1SSP_1 5'-D(*CP*TP*GP*TP*(D1P)P*AP*TP*CP*TP*T)-3' (chains A)
CTGTXATCTT

Sequence of entity 2 (B), FASTA

>1SSP_2 5'-D(*AP*AP*AP*GP*AP*TP*AP*AP*CP*AP*G)-3' (chains B)
AAAGATAACAG

Sequence of entity 3 (E), FASTA

>1SSP_3 URACIL-DNA GLYCOSYLASE (chains E)
MEFFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVI
LGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVL
LLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRH
HVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL

Ligands and cofactors

ID	Name	Formula	Copies
URA	Uracil	C4 H4 N2 O2	1

Primary citation

Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. Parikh, S.S., Mol, C.D., Slupphaug, G. et al. EMBO J (1998) 17:5214-5226. DOI 10.1093/emboj/17.17.5214 · PubMed

Other PDB entries of the same protein (UniProt P13051 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3FCI 1.27 Å, Complex of UNG2 and a fragment-based designed inhibitor
2HXM 1.3 Å, Complex of UNG2 and a small Molecule synthetic Inhibitor
3TKB 1.5 Å, crystal structure of human uracil-DNA glycosylase D183G/K302R mutant
1AKZ 1.57 Å, Human uracil-DNA glycosylase
3FCK 1.64 Å, Complex of UNG2 and a fragment-based design inhibitor
3FCL 1.7 Å, Complex of UNG2 and a fragment-based designed inhibitor
9LNQ 1.74 Å, The hUNG bound to DNA product embedding 4primer-OCH3-dU
9LNP 1.76 Å, the hUNG bound to DNA product embedding uridine ribonucleotide
1EMH 1.8 Å, Crystal structure of human uracil-DNA glycosylase bound to uncleaved…
6VBA 1.8 Å, Structure of human Uracil DNA Glycosylase (UDG) bound to Aurintricarboxylic acid (ATA)
3FCF 1.84 Å, Complex of UNG2 and a fragment-based designed inhibitor
1Q3F 1.9 Å, Uracil DNA glycosylase bound to a cationic 1-aza-2'-deoxyribose-containing DNA

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