Research workbench
Staphylococcus aureus udg / ugi complex
Analyse Staphylococcus aureus udg / ugi complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WDG
- Type
- protein
- Length
- 326 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uracil-DNA glycosylase; Uncharacterized protein
- EC
- 3.2.2.27
- UniProt
- Q6GJ88, Q936H5
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uracil-DNA glycosylase (EC 3.2.2.27) | protein | 216 | 41% helix, 12% strand | Q6GJ88 |
| B | Uncharacterized protein | protein | 110 | 25% helix, 38% strand | Q936H5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.49 | 0.84 | 20 | empty |
| 2 | 142 | 0.47 | 0.78 | 25 | empty |
| 3 | 93 | 0.34 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1274 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
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 Q6GJ88
- Every structure of UniProt Q936H5
- Elsewhere: RCSB PDB 3WDG · PDBe 3WDG · UniProt Q6GJ88 · UniProt Q936H5
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