Research workbench
3D structure of horse spleen apoferritin determined by electron cryomicroscopy
Analyse 3D structure of horse spleen apoferritin determined by electron cryomicroscopy in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V1W
- Type
- protein
- Length
- 4,080 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin light chain
- UniProt
- P02791
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 75% 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 light chain | protein | 170 | 75% helix, 1% strand | P02791 |
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 | 130 | 0.75 | 0.94 | 27 | empty |
| 2 | 157 | 0.75 | 0.93 | 33 | empty |
| 3 | 158 | 0.75 | 0.92 | 33 | empty |
| 4 | 133 | 0.75 | 0.93 | 27 | empty |
| 5 | 166 | 0.74 | 0.92 | 31 | empty |
Interfaces
72 interfaces between chains.
- K–P · 1576 Ų buried · 28 hydrogen bonds · protein-protein
- L–M · 1574 Ų buried · 28 hydrogen bonds · protein-protein
- C–J · 1574 Ų buried · 28 hydrogen bonds · protein-protein
- N–S · 1573 Ų buried · 28 hydrogen bonds · protein-protein
- H–I · 1573 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 4V1W · 3D structure of horse spleen apoferritin determined by electron cryomicroscopy · the same entry in another collection · chain J against J, 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 P02791
- Elsewhere: RCSB PDB 4V1W · PDBe 4V1W · UniProt P02791
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