Research workbench
Structure of catalytic domain of ssel
Analyse Structure of catalytic domain of ssel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UBW
- Type
- protein
- Length
- 348 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deubiquitinase ssel
- EC
- 3.4.22.-
- UniProt
- Q8ZNG2
- Pockets
- 2 · best druggability 0.54
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deubiquitinase ssel (EC 3.4.22.-) | protein | 175 | 46% helix, 18% strand | Q8ZNG2 |
| B | Deubiquitinase ssel (EC 3.4.22.-) | protein | 173 | 42% helix, 18% strand | Q8ZNG2 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 325 | 0.54 | 0.75 | 27 | empty |
| 2 | 70 | 0.38 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 250 Ų buried · 1 hydrogen bond · 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 Q8ZNG2
- Elsewhere: RCSB PDB 5UBW · PDBe 5UBW · UniProt Q8ZNG2
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