Research workbench
Crystal structure of thermotoga maritima ferritin in apo form
Analyse Crystal structure of thermotoga maritima ferritin in apo form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TXH
- Type
- protein
- Length
- 1,312 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- EC
- 1.16.3.2
- UniProt
- Q9X0L2
- Ligands
- LFA, SO4
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Ferritin (EC 1.16.3.2) | protein | 164 | 77% helix, 1% strand | Q9X0L2 |
Ligands and binding sites
- LFA · Eicosane · ligand · 4 copies · chains A, B, C, D, E, F, G, H
- SO4 · Sulfate ion · ion · 26 copies · chains A, B, D, E, C, F, G, H
- GOL · Glycerol · additive · 3 copies · chains A, B, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 773 | 0.73 | 0.78 | 76 | empty |
| 2 | 258 | 0.72 | 0.85 | 25 | LFA |
| 3 | 408 | 0.71 | 0.82 | 32 | empty |
| 4 | 271 | 0.71 | 0.85 | 28 | LFA |
| 5 | 274 | 0.70 | 0.84 | 25 | LFA |
Interfaces
13 interfaces between chains.
- A–B · 1249 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1242 Ų buried · 23 hydrogen bonds · protein-protein
- G–H · 1239 Ų buried · 27 hydrogen bonds · protein-protein
- E–F · 1229 Ų buried · 23 hydrogen bonds · protein-protein
- C–E · 558 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6TXH · Crystal structure of thermotoga maritima Ferritin in apo form · the same entry in another collection · chain H against H, 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 Q9X0L2
- Elsewhere: RCSB PDB 6TXH · PDBe 6TXH · UniProt Q9X0L2
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