Research workbench
Tryparedoxin II from C.FASCICULATA solved by mr
Analyse Tryparedoxin II from C.FASCICULATA solved by mr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OC8
- Type
- protein
- Length
- 296 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tryparedoxin II
- UniProt
- O77093
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryparedoxin II | protein | 151 | 35% helix, 23% strand | O77093 |
| B | Tryparedoxin II | protein | 145 | 34% helix, 23% strand | O77093 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 223 | 0.63 | 0.82 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 322 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1OC8 · Tryparedoxin II from C.FASCICULATA solved by mr · 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 1OC8 · PDBe 1OC8 · UniProt O77093
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