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Structure of the Usp25 C-terminal domain
Analyse Structure of the Usp25 C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H4K
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Homo sapiens
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 25
- EC
- 3.4.19.12
- UniProt
- Q9UHP3
- Ligands
- CL
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · resolution 2.05 · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 25 (EC 3.4.19.12) | protein | 270 | 73% helix, 0% strand | Q9UHP3 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.42 | 0.77 | 16 | empty |
| 2 | 113 | 0.41 | 0.76 | 23 | CL |
Modifications
Observed in the structure: 9 modified (engineered).
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 Q9UHP3
- Elsewhere: RCSB PDB 6H4K · PDBe 6H4K · UniProt Q9UHP3
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