Research workbench
Tryparedoxin II from C.FASCICULATA solved by sulphur phasing
Analyse Tryparedoxin II from C.FASCICULATA solved by sulphur phasing in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O6J
- Type
- protein
- Length
- 295 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryparedoxin II
- UniProt
- O77093
- Pockets
- 3 · best druggability 0.38
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryparedoxin II | protein | 149 | 36% helix, 23% strand | O77093 |
| B | Tryparedoxin II | protein | 146 | 35% helix, 24% strand | O77093 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 79 | 0.38 | 0.77 | 17 | empty |
| 2 | 67 | 0.32 | 0.75 | 17 | empty |
| 3 | 53 | 0.24 | 0.72 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 651 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1O6J · Tryparedoxin II from C.fasciculata solved by sulphur phasing · 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 O77093
- Elsewhere: RCSB PDB 1O6J · PDBe 1O6J · UniProt O77093
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