Research workbench
BETA1MUT synthetic solenoid protein
Analyse BETA1MUT synthetic solenoid protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4YEI
- Type
- protein
- Length
- 645 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- BETA1MUT
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | BETA1MUT | protein | 215 | 11% helix, 17% strand | — |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 975 | 0.77 | 0.80 | 102 | empty |
Interfaces
3 interfaces between chains.
- A–B · 231 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 165 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 163 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4YEI · Beta1mut synthetic solenoid protein · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 4YEI · PDBe 4YEI
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