Research workbench
Human apo ferritin frozen on TEM grid with amorphous carbon supporting film
Analyse Human apo ferritin frozen on TEM grid with amorphous carbon supporting film in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M52
- Type
- protein
- Length
- 4,104 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Homo sapiens
- Molecule
- Ferritin heavy chain
- EC
- 1.16.3.1
- UniProt
- P02794
- Ligands
- FE2
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · resolution 2.6 · 1 distinct chain · 73% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X | Ferritin heavy chain (EC 1.16.3.1) | protein | 171 | 73% helix, 1% strand | P02794 |
Ligands and binding sites
- FE2 · Fe (II) ion · metal · 6 copies · chains A, D, Q, T, B, C, R, S, E, H, M, P, F, G, N, O, I, L, V, W, J, K, U, X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.75 | 0.98 | 13 | empty |
| 2 | 69 | 0.73 | 0.97 | 14 | empty |
| 3 | 74 | 0.73 | 0.96 | 13 | empty |
| 4 | 76 | 0.73 | 0.96 | 13 | empty |
| 5 | 73 | 0.73 | 0.97 | 14 | empty |
Interfaces
60 interfaces between chains.
- D–U · 1526 Ų buried · 13 hydrogen bonds · protein-protein
- I–P · 1521 Ų buried · 13 hydrogen bonds · protein-protein
- A–V · 1519 Ų buried · 13 hydrogen bonds · protein-protein
- C–X · 1519 Ų buried · 13 hydrogen bonds · protein-protein
- B–W · 1518 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6M52 · Human apo ferritin frozen on tem grid with amorphous carbon supporting film · the same entry in another collection · chain K against K, 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 P02794
- Elsewhere: RCSB PDB 6M52 · PDBe 6M52 · UniProt P02794
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