Research workbench
Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and thioredoxin F
Analyse Crystal srtucture of the binary complex between ferredoxin: thioredoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PU9
- Type
- protein
- Length
- 295 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferredoxin-thioredoxin reductase, catalytic chain; Ferredoxin-thioredoxin reductase…
- UniProt
- Q55389, Q55781, P09856
- Ligands
- SF4, SO4
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 3 distinct chains · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-thioredoxin reductase, catalytic chain | protein | 110 | 53% helix, 6% strand | Q55389 |
| B | Ferredoxin-thioredoxin reductase, variable chain | protein | 74 | 8% helix, 41% strand | Q55781 |
| C | Thioredoxin F-type, chloroplast | protein | 111 | 36% helix, 25% strand | P09856 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 163 | 0.61 | 0.84 | 20 | SO4 |
| 2 | 233 | 0.55 | 0.77 | 39 | SF4, SO4 |
| 3 | 81 | 0.39 | 0.78 | 13 | empty |
| 4 | 71 | 0.33 | 0.75 | 12 | empty |
Interfaces
3 interfaces between chains.
- A–B · 870 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 860 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 23 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2PU9 · Crystal srtucture of the binary complex between ferredoxin: thioredoxin reductase and… · the same entry in another collection · chain A against A, TM-score 1.00
- P09856 · AlphaFold monomer V2.0 prediction for thioredoxin F-type, chloroplastic (P09856) · a predicted model of the same protein · chain C against A, TM-score 0.99
- Q55389 · AlphaFold monomer V2.0 prediction for ferredoxin-thioredoxin reductase, catalytic chain… · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q55781 · AlphaFold monomer V2.0 prediction for ferredoxin-thioredoxin reductase, variable chain… · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q55389
- Every structure of UniProt Q55781
- Every structure of UniProt P09856
- Elsewhere: RCSB PDB 2PU9 · PDBe 2PU9 · UniProt Q55389 · UniProt Q55781 · UniProt P09856
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