Research workbench
Mouse heavy chain apoferritin determined using single-particle cryo-EM at 200 kev
Analyse Mouse heavy chain apoferritin determined using single-particle cryo-EM at 200… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V21
- Type
- protein
- Length
- 4,160 residues
- Chains
- 24
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferritin heavy chain
- EC
- 1.16.3.1
- UniProt
- P09528
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 2 distinct chains · 72% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, H, I, K, M, N, O, P, Q, T, U, W | Ferritin heavy chain (EC 1.16.3.1) | protein | 173 | 72% helix, 1% strand | P09528 |
| F, G, J, L, R, S, V, X | Ferritin heavy chain (EC 1.16.3.1) | protein | 174 | 72% helix, 1% strand | P09528 |
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 | 95 | 0.79 | 0.99 | 17 | empty |
| 2 | 88 | 0.79 | 0.99 | 15 | empty |
| 3 | 96 | 0.79 | 0.98 | 18 | empty |
| 4 | 95 | 0.78 | 0.98 | 16 | empty |
| 5 | 86 | 0.78 | 0.99 | 14 | empty |
Interfaces
72 interfaces between chains.
- T–W · 1512 Ų buried · 34 hydrogen bonds · protein-protein
- C–J · 1511 Ų buried · 34 hydrogen bonds · protein-protein
- H–K · 1511 Ų buried · 34 hydrogen bonds · protein-protein
- L–S · 1510 Ų buried · 34 hydrogen bonds · protein-protein
- G–X · 1510 Ų buried · 34 hydrogen bonds · protein-protein
Compared structures
- 6V21 · Mouse heavy chain apoferritin determined using single-particle cryo-EM at 200 keV · the same entry in another collection · chain B against B, 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 P09528
- Elsewhere: RCSB PDB 6V21 · PDBe 6V21 · UniProt P09528
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