Research workbench
Mitochondrial peroxiredoxin from leishmania infantum after heat stress without unfolding client protein
Analyse Mitochondrial peroxiredoxin from leishmania infantum after heat stress without… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E0G
- Type
- protein
- Length
- 1,650 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial 2-cys-peroxiredoxin
- EC
- 1.11.1.-
- UniProt
- Q95U89
- Pockets
- 20 · best druggability 0.56
Structure
electron microscopy · 1 distinct chain · 28% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, A, B, C, D, E, F, G, H, I | Mitochondrial 2-cys-peroxiredoxin (EC 1.11.1.-) | protein | 165 | 28% helix, 26% strand | Q95U89 |
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.56 | 0.79 | 34 | empty |
| 2 | 212 | 0.56 | 0.79 | 37 | empty |
| 3 | 208 | 0.55 | 0.79 | 36 | empty |
| 4 | 188 | 0.55 | 0.79 | 34 | empty |
| 5 | 242 | 0.53 | 0.76 | 42 | empty |
Interfaces
10 interfaces between chains.
- J–A · 1116 Ų buried · 20 hydrogen bonds · protein-protein
- D–H · 1112 Ų buried · 19 hydrogen bonds · protein-protein
- C–G · 1106 Ų buried · 18 hydrogen bonds · protein-protein
- B–F · 1104 Ų buried · 20 hydrogen bonds · protein-protein
- E–I · 1102 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6E0G · Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding… · 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 Q95U89
- Elsewhere: RCSB PDB 6E0G · PDBe 6E0G · UniProt Q95U89
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