Research workbench
Tryparedoxin peroxidase from crithidia fasciculata
Analyse Tryparedoxin peroxidase from crithidia fasciculata in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1E2Y
- Type
- protein
- Length
- 1,678 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9TZX2
Structure
x-ray diffraction · 8 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 167 | — | Q9TZX2 |
| B | — | protein | 171 | — | Q9TZX2 |
| C, I | — | protein | 170 | — | Q9TZX2 |
| D, J | — | protein | 166 | — | Q9TZX2 |
| E | — | protein | 165 | — | Q9TZX2 |
| F | — | protein | 161 | — | Q9TZX2 |
| G | — | protein | 173 | — | Q9TZX2 |
| H | — | protein | 169 | — | Q9TZX2 |
Compared structures
- 1E2Y · Tryparedoxin peroxidase from Crithidia fasciculata · the same entry in another collection · chain A 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 Q9TZX2
- Elsewhere: RCSB PDB 1E2Y · PDBe 1E2Y · UniProt Q9TZX2
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