A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1. Determined by X-ray diffraction at 2.1 Å resolution. Released 28 Nov 2005.
Explore 2C56 in 3D Show helices and sheets RCSB PDB PDBe
2C56 contains 15 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-26 | 8 | |
| α-helix | 30-32 | 3 | |
| α-helix | 33-36 | 4 | |
| α-helix | 37-41 | 5 | |
| α-helix | 43-58 | 16 | |
| β-strand | 61-62 | 2 | 1 |
| α-helix | 65-67 | 3 | |
| α-helix | 71-74 | 4 | |
| α-helix | 77-79 | 3 | |
| β-strand | 82-86 | 5 | 2 |
| α-helix | 108-110 | 3 | |
| α-helix | 111-123 | 13 | |
| α-helix | 136-140 | 5 | |
| β-strand | 143-147 | 5 | 2 |
| β-strand | 152-153 | 2 | 1 |
| β-strand | 156 | 1 | 1 |
| α-helix | 165-179 | 15 | |
| β-strand | 184-188 | 5 | 2 |
| α-helix | 190-195 | 6 | |
| β-strand | 204-208 | 5 | 2 |
| α-helix | 224-234 | 11 | |
| α-helix | 238-240 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uracil DNA glycosylase | A | protein | 244 | HUMAN HERPESVIRUS 1 | P10186 |
>2C56_1 URACIL DNA GLYCOSYLASE (chains A) MDLTNGGVSPAATSAPLDWTTFRRVFLIDDAWRPLMEPELANPLTAHLLAEYNRRCQTEE VLPPREDVFSWTRYCTPDEVRVVIIGQNPYHHPGQAHGLAFSVRANVPPPPSLRNVLAAV KNCYPEARMSGHGCLEKWARDGVLLLNTTLTVKRGAAASHSRIGWDRFVGGVIRRLAARR PGLVFMLWGTHAQNAIRPDPRVHCVLKFSNPSPLSKVPFGTCQHFLVANRYLETRSISPI DWSV
A Comparative Study of Uracil-DNA Glycosylases from Human and Herpes Simplex Virus Type 1. Krusong, K., Carpenter, E.P., Bellamy, S.R.W. et al. J Biol Chem (2006) 281:4983. DOI 10.1074/JBC.M509137200 · PubMed
Other PDB entries of the same protein (UniProt P10186), best resolution first:
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