Research workbench
Crystal structure of Ferritin 2 from Caenorhabditis elegans, FTN-2
Analyse Crystal structure of Ferritin 2 from Caenorhabditis elegans, FTN-2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7URH
- Type
- protein
- Length
- 1,008 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.468
- Source
- Caenorhabditis elegans
- Molecule
- Ferritin
- EC
- 1.16.3.1
- UniProt
- Q9TYS3
- Ligands
- FE
- Pockets
- 5 · best druggability 0.76
Structure
x-ray diffraction · resolution 1.468 · 1 distinct chain · 74% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Ferritin (EC 1.16.3.1) | protein | 168 | 74% helix, 1% strand | Q9TYS3 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 6 copies · chains A, C, E, G, I, K
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 3 copies · chains A, C, E, I, G, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.76 | 0.98 | 15 | MPD |
| 2 | 67 | 0.76 | 0.99 | 14 | MPD |
| 3 | 63 | 0.75 | 0.99 | 14 | MPD |
| 4 | 156 | 0.45 | 0.76 | 27 | empty |
| 5 | 71 | 0.29 | 0.73 | 17 | empty |
Interfaces
7 interfaces between chains.
- A–C · 1540 Ų buried · 24 hydrogen bonds · protein-protein
- E–I · 1528 Ų buried · 27 hydrogen bonds · protein-protein
- G–K · 1498 Ų buried · 27 hydrogen bonds · protein-protein
- E–G · 705 Ų buried · 5 hydrogen bonds · protein-protein
- C–I · 702 Ų buried · 5 hydrogen bonds · protein-protein
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 Q9TYS3
- Elsewhere: RCSB PDB 7URH · PDBe 7URH · UniProt Q9TYS3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.