Research workbench
Optimisation of the surface electrostatics as a strategy for cold adaptation of uracil-DNA N-glycosylase (UNG)FROM atlantic cod (gadus morhua)
Analyse Optimisation of the surface electrostatics as a strategy for cold adaptation of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YUO
- Type
- protein
- Length
- 223 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
- P13051
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uracil-DNA glycosylase (EC 3.2.2.3) | protein | 223 | 40% helix, 11% strand | P13051 |
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 | 125 | 0.48 | 0.79 | 29 | empty |
Compared structures
- 1YUO · Optimisation of the surface electrostatics as a strategy for cold adaptation of… · the same entry in another collection · chain A against A, TM-score 1.00
- P13051 · AlphaFold monomer V2.0 prediction for uracil-DNA glycosylase (P13051) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P13051
- Elsewhere: RCSB PDB 1YUO · PDBe 1YUO · UniProt P13051
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