Research workbench
Crystal srtucture of the binary complex between ferredoxin and FERREDOXIN:THIOREDOXIN reductase
Analyse Crystal srtucture of the binary complex between ferredoxin and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PVG
- Type
- protein
- Length
- 277 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, P27320
- Ligands
- SF4, FES
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 27% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferredoxin-thioredoxin reductase, catalytic chain | protein | 108 | 50% helix, 6% strand | Q55389 |
| B | Ferredoxin-thioredoxin reductase, variable chain | protein | 73 | 4% helix, 42% strand | Q55781 |
| C | Ferredoxin-1 | protein | 96 | 18% helix, 34% strand | P27320 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 424 | 0.67 | 0.79 | 39 | empty |
| 2 | 100 | 0.35 | 0.74 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 960 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 655 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 21 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2PVG · Crystal srtucture of the binary complex between ferredoxin and ferredoxin:thioredoxin… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.99
- P27320 · AlphaFold monomer V2.0 prediction for ferredoxin-1 (P27320) · a predicted model of the same protein · chain C against A, TM-score 0.99
- 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 0.93
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 P27320
- Elsewhere: RCSB PDB 2PVG · PDBe 2PVG · UniProt Q55389 · UniProt Q55781 · UniProt P27320
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