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Crystal structure of the highly amyloidogenic transthyretin mutant ttr G53S/E54D/L55S- heated protein
Analyse Crystal structure of the highly amyloidogenic transthyretin mutant ttr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2QEL
- Type
- protein
- Length
- 459 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Pockets
- 8 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 6% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transthyretin | protein | 115 | 5% helix, 55% strand | P02766 |
| B | Transthyretin | protein | 114 | 5% helix, 57% strand | P02766 |
| C | Transthyretin | protein | 114 | 5% helix, 50% strand | P02766 |
| D | Transthyretin | protein | 116 | 7% helix, 55% strand | P02766 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 331 | 0.82 | 0.92 | 64 | empty |
| 2 | 379 | 0.69 | 0.82 | 42 | empty |
| 3 | 55 | 0.43 | 0.83 | 20 | empty |
| 4 | 80 | 0.40 | 0.78 | 17 | empty |
| 5 | 115 | 0.37 | 0.73 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 940 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 939 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 613 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 401 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 350 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 2QEL · Crystal structure of the highly amyloidogenic transthyretin mutant TTR G53S/E54D/L55S… · 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 P02766
- Elsewhere: RCSB PDB 2QEL · PDBe 2QEL · UniProt P02766
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