Research workbench
Human transthyretin (ttr) complexed with ferulic acid and curcumin.
Analyse Human transthyretin (ttr) complexed with ferulic acid and curcumin. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PME
- Type
- protein
- Length
- 233 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transthyretin
- UniProt
- P02766
- Ligands
- FER, CUR, NA
- Pockets
- 3 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transthyretin | protein | 117 | 6% helix, 50% strand | P02766 |
| B | Transthyretin | protein | 116 | 6% helix, 51% strand | P02766 |
Ligands and binding sites
- FER · 3-(4-hydroxy-3-methoxyphenyl)-2-propenoic acid · ligand · 2 copies · chains B
- CUR · (1Z,4Z,6E)-5-hydroxy-1,7-bis(4-hydroxy-3-methoxyphenyl)hepta-1,4,6-trien-3-one · ligand · chains A
- NA · Sodium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 74 | 0.35 | 0.76 | 19 | empty |
| 2 | 75 | 0.34 | 0.76 | 17 | empty |
| 3 | 56 | 0.27 | 0.73 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 890 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 4PME · Human transthyretin (TTR) complexed with ferulic acid and curcumin. · 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 4PME · PDBe 4PME · UniProt P02766
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