Research workbench
Crystal structure of escherichia COLI uracil DNA glycosylase and its complexes with uracil and glycerol: structure and glycosylase mechanism revisited
Analyse Crystal structure of escherichia COLI uracil DNA glycosylase and its complexes… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EUG
- Type
- protein
- Length
- 225 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (glycosylase)
- EC
- 3.2.2.3
- UniProt
- P12295
- Pockets
- 1 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (glycosylase) (EC 3.2.2.3) | protein | 225 | 38% helix, 11% strand | P12295 |
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 | 147 | 0.53 | 0.80 | 33 | empty |
Compared structures
- 1EUG · Crystal structure of escherichia COLI uracil DNA glycosylase and its complexes with… · the same entry in another collection · chain A against A, TM-score 1.00
- P12295 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P12295) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P12295
- Elsewhere: RCSB PDB 1EUG · PDBe 1EUG · UniProt P12295
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