Research workbench
Cryo-EM structure of alpha 7 homo-tetradecamer
Analyse Cryo-EM structure of alpha 7 homo-tetradecamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E55
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit alpha type-3
- UniProt
- P25788
- Pockets
- 3 · best druggability 0.40
Structure
electron microscopy · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proteasome subunit alpha type-3 | protein | 244 | 36% helix, 21% strand | P25788 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.40 | 0.77 | 25 | empty |
| 2 | 67 | 0.40 | 0.80 | 15 | empty |
| 3 | 65 | 0.36 | 0.78 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P25788
- Elsewhere: RCSB PDB 7E55 · PDBe 7E55 · UniProt P25788
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