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Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation damage effect at 3.4 MGy, focused in disulfide bonds.
Analyse Crystallographic structure of thioredoxin from Litopenaeus vannamei: Radiation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4V2L
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.65
- Source
- LITOPENAEUS VANNAMEI
- Molecule
- Thioredoxin
- EC
- 1.8.1.9
- UniProt
- B1PWB9
- Ligands
- SO4
Structure
x-ray diffraction · resolution 1.65 · 1 distinct chain · 41% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Thioredoxin (EC 1.8.1.9) | protein | 105 | 41% helix, 29% strand | B1PWB9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains B
- GOL · Glycerol · additive · 2 copies · chains A
- ACT · Acetate ion · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 690 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 4V2L · Crystallographic structure of thioredoxin from litopenaeus vannamei: radiation damage… · 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 B1PWB9
- Elsewhere: RCSB PDB 4V2L · PDBe 4V2L · UniProt B1PWB9
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