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Crystal structure of semet VPS75
Analyse Crystal structure of semet VPS75 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C9B
- Type
- protein
- Length
- 397 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein 75
- UniProt
- P53853
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein 75 | protein | 198 | 51% helix, 16% strand | P53853 |
| B | Vacuolar protein sorting-associated protein 75 | protein | 199 | 51% helix, 16% 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 | 216 | 0.58 | 0.79 | 34 | empty |
| 2 | 246 | 0.56 | 0.78 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 1406 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 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 P53853
- Elsewhere: RCSB PDB 3C9B · PDBe 3C9B · UniProt P53853
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