Research workbench
Crystal structure of yeast RPN14
Analyse Crystal structure of yeast RPN14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VL1
- Type
- protein
- Length
- 832 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 26S proteasome regulatory subunit RPN14
- UniProt
- P53196
- Pockets
- 12 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 26S proteasome regulatory subunit RPN14 | protein | 416 | 2% helix, 49% strand | P53196 |
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.81 | 0.93 | 68 | empty |
| 2 | 388 | 0.72 | 0.83 | 47 | empty |
| 3 | 294 | 0.68 | 0.83 | 40 | empty |
| 4 | 433 | 0.64 | 0.77 | 50 | empty |
| 5 | 364 | 0.61 | 0.77 | 46 | empty |
Interfaces
1 interface between chains.
- A–B · 2160 Ų buried · 24 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 P53196
- Elsewhere: RCSB PDB 3VL1 · PDBe 3VL1 · UniProt P53196
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