Research workbench
Mitochondrial peroxiredoxin from leishmania infantum in complex with unfolding client protein after heat stress
Analyse Mitochondrial peroxiredoxin from leishmania infantum in complex with unfolding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6E0F
- Type
- protein
- Length
- 1,740 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 0.70
Structure
electron microscopy · 1 distinct chain · 22% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, A, I, E, G, F, B, C, D, H | Mitochondrial 2-cys-peroxiredoxin (EC 1.11.1.-) | protein | 174 | 22% helix, 24% strand | Q95U89 |
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 526 | 0.70 | 0.80 | 61 | empty |
| 2 | 425 | 0.69 | 0.81 | 46 | empty |
| 3 | 426 | 0.69 | 0.81 | 49 | empty |
| 4 | 433 | 0.69 | 0.80 | 46 | empty |
| 5 | 440 | 0.68 | 0.80 | 47 | empty |
Interfaces
10 interfaces between chains.
- D–H · 1390 Ų buried · 23 hydrogen bonds · protein-protein
- F–B · 1387 Ų buried · 23 hydrogen bonds · protein-protein
- G–C · 1381 Ų buried · 23 hydrogen bonds · protein-protein
- J–A · 1367 Ų buried · 24 hydrogen bonds · protein-protein
- I–E · 1331 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 6E0F · Mitochondrial peroxiredoxin from Leishmania infantum in complex with unfolding client… · 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 6E0F · PDBe 6E0F · UniProt Q95U89
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