Research workbench
The X-ray crystal structure refinements of normal human transthyretin and the amyloidogenic val 30-->met variant to 1.7 ångströms resolution
Analyse The X-ray crystal structure refinements of normal human transthyretin and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ETB
- Type
- protein
- Length
- 235 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Ligands
- T44
- Pockets
- 4 · best druggability 0.33
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Transthyretin | protein | 118 | 6% helix, 52% strand | P02766 |
| 2 | Transthyretin | protein | 117 | 6% helix, 52% strand | P02766 |
Ligands and binding sites
- T44 · 3,5,3',5'-tetraiodo-L-thyronine · ligand · 2 copies · chains 1, 2
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 73 | 0.33 | 0.75 | 15 | empty |
| 2 | 68 | 0.33 | 0.76 | 14 | empty |
| 3 | 51 | 0.31 | 0.77 | 16 | empty |
| 4 | 56 | 0.28 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- 1–2 · 925 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 1ETB · The X-ray crystal structure refinements of normal human transthyretin and the… · the same entry in another collection · chain 1 against 1, 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 1ETB · PDBe 1ETB · UniProt P02766
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