MolNFT v1 · #108292 · protein
Crystallographic structure of thioredoxin from litopenaeus vannamei: radiation damage effect at 3.4 mgy, focused in disulfide bonds.
4V2L: “Crystallographic structure of thioredoxin from litopenaeus vannamei: radiation damage effect at 3.4 mgy…”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #108292 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4V2L
- Type
- protein
- Length
- 210 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin
- EC
- 1.8.1.9
- UniProt
- B1PWB9
- Ligands
- SO4
Structure
x-ray diffraction · 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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