Research workbench
Crystal structure of thioredoxin mutant G74S
Analyse Crystal structure of thioredoxin mutant G74S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FCH
- Type
- protein
- Length
- 745 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin 1
- UniProt
- P0AA25
- Pockets
- 9 · best druggability 0.74
Structure
x-ray diffraction · 3 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, F | Thioredoxin 1 | protein | 106 | 33% helix, 27% strand | P0AA25 |
| C | Thioredoxin 1 | protein | 106 | 35% helix, 27% strand | P0AA25 |
| D, E, G | Thioredoxin 1 | protein | 107 | 35% helix, 27% strand | P0AA25 |
Ligands and binding sites
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 7 copies · chains A, B, D, C, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.74 | 0.78 | 99 | empty |
| 2 | 728 | 0.73 | 0.79 | 72 | MPD |
| 3 | 201 | 0.72 | 0.88 | 33 | MPD |
| 4 | 108 | 0.66 | 0.90 | 22 | MPD |
| 5 | 314 | 0.66 | 0.81 | 27 | empty |
Interfaces
10 interfaces between chains.
- C–F · 709 Ų buried · 22 hydrogen bonds · protein-protein
- A–E · 627 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 553 Ų buried · 11 hydrogen bonds · protein-protein
- B–C · 432 Ų buried · 1 hydrogen bond · protein-protein
- A–F · 431 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
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 P0AA25
- Elsewhere: RCSB PDB 2FCH · PDBe 2FCH · UniProt P0AA25
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