Research workbench
Coiled-coil protein
Analyse Coiled-coil protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LXO
- Type
- protein
- Length
- 634 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transforming acidic coiled-coil-containing protein 3
- UniProt
- Q9Y6A5
- Ligands
- SO4, CL
- Pockets
- 11 · best druggability 0.54
Structure
x-ray diffraction · 5 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, G | Transforming acidic coiled-coil-containing protein 3 | protein | 80 | 98% helix, 0% strand | Q9Y6A5 |
| B | Transforming acidic coiled-coil-containing protein 3 | protein | 80 | 96% helix, 0% strand | Q9Y6A5 |
| C, E | Transforming acidic coiled-coil-containing protein 3 | protein | 81 | 96% helix, 0% strand | Q9Y6A5 |
| D, F | Transforming acidic coiled-coil-containing protein 3 | protein | 77 | 92% helix, 0% strand | Q9Y6A5 |
| H | Transforming acidic coiled-coil-containing protein 3 | protein | 78 | 92% helix, 0% strand | Q9Y6A5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion
- CL · Chloride ion · ion · chains D
- PGE · Triethylene glycol · additive · 2 copies · chains A, B, D, E
- ACT · Acetate ion · additive · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 271 | 0.54 | 0.76 | 39 | empty |
| 2 | 280 | 0.53 | 0.75 | 37 | PGE |
| 3 | 146 | 0.51 | 0.79 | 18 | empty |
| 4 | 210 | 0.51 | 0.76 | 26 | empty |
| 5 | 119 | 0.42 | 0.76 | 20 | empty |
Interfaces
17 interfaces between chains.
- E–F · 1871 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 1833 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1754 Ų buried · 8 hydrogen bonds · protein-protein
- G–H · 1673 Ų buried · 10 hydrogen bonds · protein-protein
- F–H · 1163 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified, 4 disulfide (engineered, disulfide).
Compared structures
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 Q9Y6A5
- Elsewhere: RCSB PDB 5LXO · PDBe 5LXO · UniProt Q9Y6A5
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