MolNFT v1 · #118031 · protein
Crystal structure of S. cerevisiae TSA2 in the disulfide state
5EPT · Peroxiredoxin TSA2: “Crystal structure of S. cerevisiae TSA2 in the disulfide state”. X-ray diffraction, 20 pockets (best druggability 0.74). MolNFT v1 #118031 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5EPT
- Type
- protein
- Length
- 1,743 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxiredoxin TSA2
- EC
- 1.11.1.15
- UniProt
- Q04120
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 6 distinct chains · 29% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H, E | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 178 | 30% helix, 26% strand | Q04120 |
| B | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 173 | 28% helix, 25% strand | Q04120 |
| C | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 172 | 28% helix, 24% strand | Q04120 |
| A, G, J | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 175 | 29% helix, 25% strand | Q04120 |
| I | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 177 | 30% helix, 24% strand | Q04120 |
| D, F | Peroxiredoxin TSA2 (EC 1.11.1.15) | protein | 170 | 29% helix, 27% strand | Q04120 |
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.74 | 0.94 | 27 | empty |
| 2 | 391 | 0.71 | 0.82 | 58 | empty |
| 3 | 266 | 0.71 | 0.85 | 40 | empty |
| 4 | 438 | 0.70 | 0.81 | 62 | empty |
| 5 | 337 | 0.69 | 0.82 | 39 | empty |
Interfaces
10 interfaces between chains.
- B–A · 1226 Ų buried · 20 hydrogen bonds · protein-protein
- I–J · 1178 Ų buried · 17 hydrogen bonds · protein-protein
- E–F · 1124 Ų buried · 17 hydrogen bonds · protein-protein
- H–G · 1042 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 957 Ų buried · 15 hydrogen bonds · 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 Q04120
- Elsewhere: RCSB PDB 5EPT · PDBe 5EPT · UniProt Q04120
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