Research workbench
Crystal structure of uracil-DNA glycosylase (TM0511) from thermotoga maritima at 1.90 a resolution
Analyse Crystal structure of uracil-DNA glycosylase (TM0511) from thermotoga maritima… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VK2
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uracil-DNA glycosylase TM0511
- EC
- 3.2.2.-
- UniProt
- Q9WYY1
- Ligands
- SF4, UNL
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uracil-DNA glycosylase TM0511 (EC 3.2.2.-) | protein | 190 | 49% helix, 12% strand | Q9WYY1 |
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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.49 | 0.78 | 31 | UNL |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1VK2 · Crystal structure of Uracil-DNA glycosylase (TM0511) from Thermotoga maritima at 1.90 A… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9WYY1 · AlphaFold monomer V2.0 prediction for type-4 uracil-DNA glycosylase (Q9WYY1) · 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 Q9WYY1
- Elsewhere: RCSB PDB 1VK2 · PDBe 1VK2 · UniProt Q9WYY1
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