Research workbench
Crystal structure of the atypical poplar thioredoxin-LIKE2.1 in complex with gluathione
Analyse Crystal structure of the atypical poplar thioredoxin-LIKE2.1 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NYN
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin-like protein 2.1
- UniProt
- I0BZV0
- Ligands
- GSH, SO4
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-like protein 2.1 | protein | 119 | 44% helix, 23% strand | I0BZV0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 5NYN · Crystal structure of the atypical poplar thioredoxin-like2.1 in complex with gluathione · 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 I0BZV0
- Elsewhere: RCSB PDB 5NYN · PDBe 5NYN · UniProt I0BZV0
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