Research workbench
Ferritin with gc mtre LOOP2 inserted at the N-terminus
Analyse Ferritin with gc mtre LOOP2 inserted at the N-terminus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U1B
- Type
- protein
- Length
- 1,332 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mtre PROTEIN,FERRITIN chimera
- EC
- 1.16.3.2
- UniProt
- Q51006, O69434
- Pockets
- 12 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | Mtre PROTEIN,FERRITIN chimera (EC 1.16.3.2) | protein | 168 | 78% helix, 1% strand | Q51006, O69434 |
| B, C, D, E, F, G | Mtre PROTEIN,FERRITIN chimera (EC 1.16.3.2) | protein | 166 | 79% helix, 1% strand | Q51006, O69434 |
Pockets
12 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.56 | 0.82 | 29 | empty |
| 2 | 271 | 0.54 | 0.76 | 35 | empty |
| 3 | 235 | 0.51 | 0.76 | 35 | empty |
| 4 | 193 | 0.49 | 0.76 | 23 | empty |
| 5 | 162 | 0.48 | 0.77 | 23 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1247 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1232 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1220 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 1206 Ų buried · 10 hydrogen bonds · protein-protein
- A–H · 556 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5U1B · Ferritin with Gc MtrE loop2 inserted at the N-terminus · 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 Q51006
- Every structure of UniProt O69434
- Elsewhere: RCSB PDB 5U1B · PDBe 5U1B · UniProt Q51006 · UniProt O69434
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