Research workbench
Substituting hydrophobic residues for a buried salt bridge enhances protein stability but does not reduce conformational specificity
Analyse Substituting hydrophobic residues for a buried salt bridge enhances protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MYL
- Type
- protein
- Length
- 256 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arc repressor
- UniProt
- P03050
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 4 distinct chains · 63% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arc repressor | protein | 45 | 62% helix, 11% strand | P03050 |
| B, F | Arc repressor | protein | 40 | 60% helix, 13% strand | P03050 |
| C, D | Arc repressor | protein | 45 | 62% helix, 11% strand | P03050 |
| E | Arc repressor | protein | 41 | 68% helix, 12% strand | P03050 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 143 | 0.50 | 0.79 | 23 | empty |
| 2 | 161 | 0.46 | 0.76 | 28 | empty |
Interfaces
10 interfaces between chains.
- C–D · 1631 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 1569 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 1450 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 217 Ų buried · 5 hydrogen bonds · protein-protein
- D–E · 167 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1MYL · Substituting hydrophobic residues for a buried salt bridge enhances protein stability but… · 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
- Every structure of UniProt P03050
- Elsewhere: RCSB PDB 1MYL · PDBe 1MYL · UniProt P03050
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