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Crystal structure of Vps75
Analyse Crystal structure of Vps75 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C9D
- Type
- protein
- Length
- 413 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Saccharomyces cerevisiae
- Molecule
- Vacuolar protein sorting-associated protein 75
- UniProt
- P53853
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · resolution 2 · 2 distinct chains · 52% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 75 | protein | 208 | 51% helix, 15% strand | P53853 |
| B | Vacuolar protein sorting-associated protein 75 | protein | 205 | 52% helix, 15% strand | P53853 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 310 | 0.58 | 0.77 | 36 | empty |
| 2 | 142 | 0.50 | 0.79 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1432 Ų buried · 7 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 P53853
- Elsewhere: RCSB PDB 3C9D · PDBe 3C9D · UniProt P53853
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