Research workbench
Structure of human ferritin L chain
Analyse Structure of human ferritin L chain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FG8
- Type
- protein
- Length
- 1,392 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin light chain
- UniProt
- P02792
- Ligands
- CS
- Pockets
- 18 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Ferritin light chain | protein | 174 | 73% helix, 1% strand | P02792 |
Ligands and binding sites
- CS · Cesium ion · metal · 10 copies · chains A, C, D, E, H, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.73 | 0.92 | 28 | empty |
| 2 | 143 | 0.72 | 0.91 | 29 | empty |
| 3 | 147 | 0.70 | 0.90 | 31 | empty |
| 4 | 240 | 0.59 | 0.80 | 34 | CS |
| 5 | 207 | 0.55 | 0.79 | 36 | empty |
Interfaces
14 interfaces between chains.
- E–F · 1595 Ų buried · 33 hydrogen bonds · protein-protein
- B–H · 1582 Ų buried · 24 hydrogen bonds · protein-protein
- A–D · 1581 Ų buried · 29 hydrogen bonds · protein-protein
- E–H · 694 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 684 Ų buried · 7 hydrogen bonds · protein-protein
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 P02792
- Elsewhere: RCSB PDB 2FG8 · PDBe 2FG8 · UniProt P02792
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