Research workbench
Crystal structure of ferritin (TM1128) from thermotoga maritima at 2.00 a resolution
Analyse Crystal structure of ferritin (TM1128) from thermotoga maritima at 2.00 a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VLG
- Type
- protein
- Length
- 1,312 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin
- UniProt
- Q9X0L2
- Ligands
- FE, SO4
- Pockets
- 18 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Ferritin | protein | 164 | 78% helix, 1% strand | Q9X0L2 |
Ligands and binding sites
- FE · Fe (III) ion · metal · 8 copies · chains A, B, C, D, E, F, G, H
- SO4 · Sulfate ion · ion · 14 copies · chains A, C, B, D, E, F, H
- GOL · Glycerol · additive · 9 copies · chains B, C, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 486 | 0.76 | 0.84 | 29 | empty |
| 2 | 256 | 0.71 | 0.85 | 28 | empty |
| 3 | 260 | 0.71 | 0.85 | 26 | empty |
| 4 | 261 | 0.70 | 0.84 | 27 | empty |
| 5 | 591 | 0.68 | 0.77 | 61 | empty |
Interfaces
12 interfaces between chains.
- A–F · 1266 Ų buried · 33 hydrogen bonds · protein-protein
- B–E · 1266 Ų buried · 27 hydrogen bonds · protein-protein
- C–D · 1263 Ų buried · 27 hydrogen bonds · protein-protein
- G–H · 1218 Ų buried · 27 hydrogen bonds · protein-protein
- D–E · 531 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1VLG · Crystal structure of Ferritin (TM1128) from Thermotoga maritima at 2.00 A resolution · 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 Q9X0L2
- Elsewhere: RCSB PDB 1VLG · PDBe 1VLG · UniProt Q9X0L2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.