MolNFT v1 · #32934 · protein
A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1
2C53: “A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1”. X-ray diffraction, 1 ligand (DUR), 1 pocket (best druggability 0.58). MolNFT v1 #32934 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 2C53
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uracil DNA glycosylase
- EC
- 3.2.2.3
- UniProt
- P10186
- Ligands
- DUR
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uracil DNA glycosylase (EC 3.2.2.3) | protein | 228 | 42% helix, 11% strand | P10186 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.58 | 0.80 | 33 | DUR |
Compared structures
- 2C53 · A comparative study of uracil DNA glycosylases from human and herpes simplex virus type 1 · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P10186
- Elsewhere: RCSB PDB 2C53 · PDBe 2C53 · UniProt P10186
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