Research workbench
Crystal structure of full-length human peroxiredoxin 4 with T118E mutation
Analyse Crystal structure of full-length human peroxiredoxin 4 with T118E mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TKR
- Type
- protein
- Length
- 1,968 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peroxiredoxin-4
- EC
- 1.11.1.15
- UniProt
- Q13162
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, I, C, F, D, B, H, E, J | Peroxiredoxin-4 (EC 1.11.1.15) | protein | 197 | 30% helix, 26% strand | Q13162 |
| G | Peroxiredoxin-4 (EC 1.11.1.15) | protein | 195 | 31% helix, 26% strand | Q13162 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.72 | 0.99 | 23 | empty |
| 2 | 50 | 0.71 | 0.99 | 21 | empty |
| 3 | 302 | 0.68 | 0.83 | 44 | empty |
| 4 | 312 | 0.68 | 0.82 | 44 | empty |
| 5 | 315 | 0.68 | 0.82 | 33 | empty |
Interfaces
20 interfaces between chains.
- A–I · 2371 Ų buried · 37 hydrogen bonds · protein-protein
- F–D · 2368 Ų buried · 32 hydrogen bonds · protein-protein
- E–J · 2343 Ų buried · 35 hydrogen bonds · protein-protein
- G–C · 2231 Ų buried · 32 hydrogen bonds · protein-protein
- B–H · 2212 Ų buried · 31 hydrogen bonds · protein-protein
Compared structures
- 3TKR · Crystal structure of full-length human peroxiredoxin 4 with T118E mutation · the same entry in another collection · chain J against J, TM-score 1.00
- Q13162 · AlphaFold monomer V2.0 prediction for peroxiredoxin-4 (Q13162) · a predicted model of the same protein · chain G 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 Q13162
- Elsewhere: RCSB PDB 3TKR · PDBe 3TKR · UniProt Q13162
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