Research workbench
Crystal structure of full-length human peroxiredoxin 4 in the reduced form
Analyse Crystal structure of full-length human peroxiredoxin 4 in the reduced form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TKP
- Type
- protein
- Length
- 982 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q13162
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 197 | — | Q13162 |
| C | — | protein | 195 | — | Q13162 |
| E | — | protein | 196 | — | Q13162 |
Compared structures
- 3TKP · Crystal structure of full-length human peroxiredoxin 4 in the reduced form · the same entry in another collection · chain E against E, TM-score 1.00
- Q13162 · AlphaFold monomer V2.0 prediction for peroxiredoxin-4 (Q13162) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 3TKP · PDBe 3TKP · UniProt Q13162
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