Research workbench
Ferritin with gc mtre loop 1 inserted at HIS34
Analyse Ferritin with gc mtre loop 1 inserted at HIS34 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5U1A
- Type
- protein
- Length
- 2,018 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FERRITIN,MTRE protein chimera
- EC
- 1.16.3.2
- UniProt
- A0A0B2EHC8, Q51006
- Ligands
- NA, FE, CL
- Pockets
- 20 · best druggability 0.57
Structure
x-ray diffraction · 10 distinct chains · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 169 | 78% helix, 1% strand | A0A0B2EHC8, Q51006 |
| B, H | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 167 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
| C | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 168 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
| D | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 169 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
| E | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 169 | 78% helix, 1% strand | A0A0B2EHC8, Q51006 |
| F | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 168 | 78% helix, 1% strand | A0A0B2EHC8, Q51006 |
| G | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 170 | 78% helix, 1% strand | A0A0B2EHC8, Q51006 |
| I | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 169 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
| J, K | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 168 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
| L | FERRITIN,MTRE protein chimera (EC 1.16.3.2) | protein | 166 | 79% helix, 1% strand | A0A0B2EHC8, Q51006 |
Ligands and binding sites
- NA · Sodium ion · metal · 30 copies · chains A, B, C, D, E, F, G, L, H, J, K, I
- FE · Fe (III) ion · metal · 6 copies · chains A, B, D, E, F, G, H, J, K, L
- CL · Chloride ion · ion · 8 copies · chains C, D, F, G, K, L
- GOL · Glycerol · additive · 12 copies · chains B, E, C, D, A, F, H, K, I, J, G, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 158 | 0.57 | 0.82 | 31 | empty |
| 2 | 178 | 0.57 | 0.81 | 33 | empty |
| 3 | 289 | 0.55 | 0.76 | 40 | GOL |
| 4 | 262 | 0.54 | 0.76 | 32 | empty |
| 5 | 234 | 0.52 | 0.76 | 33 | empty |
Interfaces
16 interfaces between chains.
- C–D · 1320 Ų buried · 13 hydrogen bonds · protein-protein
- H–K · 1320 Ų buried · 14 hydrogen bonds · protein-protein
- I–J · 1284 Ų buried · 14 hydrogen bonds · protein-protein
- B–E · 1280 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 1253 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 5U1A · Ferritin with Gc MtrE loop 1 inserted at His34 · 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 A0A0B2EHC8
- Every structure of UniProt Q51006
- Elsewhere: RCSB PDB 5U1A · PDBe 5U1A · UniProt A0A0B2EHC8 · UniProt Q51006
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