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Crystal structure of TM1086
Analyse Crystal structure of TM1086 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DCL
- Type
- protein
- Length
- 1,408 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- TM1086
- UniProt
- Q9X0H2
- Ligands
- K, SO4, CL
- Pockets
- 17 · best druggability 0.66
Structure
x-ray diffraction · 5 distinct chains · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TM1086 | protein | 283 | 11% helix, 37% strand | Q9X0H2 |
| B | TM1086 | protein | 281 | 11% helix, 38% strand | Q9X0H2 |
| C | TM1086 | protein | 280 | 11% helix, 38% strand | Q9X0H2 |
| D | TM1086 | protein | 282 | 11% helix, 37% strand | Q9X0H2 |
| E | TM1086 | protein | 282 | 11% helix, 38% strand | Q9X0H2 |
Ligands and binding sites
- K · Potassium ion · metal · 5 copies · chains A, B, C, D, E
- SO4 · Sulfate ion · ion · 14 copies · chains A, B, C, D, E
- CL · Chloride ion · ion · 12 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 188 | 0.66 | 0.85 | 21 | empty |
| 2 | 186 | 0.65 | 0.85 | 21 | empty |
| 3 | 175 | 0.64 | 0.85 | 22 | empty |
| 4 | 166 | 0.64 | 0.85 | 23 | empty |
| 5 | 121 | 0.63 | 0.87 | 25 | empty |
Interfaces
5 interfaces between chains.
- B–C · 1360 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1327 Ų buried · 13 hydrogen bonds · protein-protein
- C–E · 1326 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 1321 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1302 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 55 modified (engineered).
Compared structures
- 3DCL · Crystal structure of TM1086 · 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 Q9X0H2
- Elsewhere: RCSB PDB 3DCL · PDBe 3DCL · UniProt Q9X0H2
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