MolNFT v1 · #24885 · protein
Crystal structure analysis of thioredoxin from thermus thermophilus
1V98: “Crystal structure analysis of thioredoxin from thermus thermophilus”. X-ray diffraction, 2 ligands (MG, SO4), 1 pocket (best druggability 0.31). MolNFT v1 #24885 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1V98
- Type
- protein
- Length
- 181 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin
- EC
- 1.8.1.9
- UniProt
- Q5SI93
- Ligands
- MG, SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin (EC 1.8.1.9) | protein | 92 | 37% helix, 29% strand | Q5SI93 |
| B | Thioredoxin (EC 1.8.1.9) | protein | 89 | 38% helix, 30% strand | Q5SI93 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.31 | 0.74 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 462 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1V98 · Crystal Structure Analysis of Thioredoxin from Thermus thermophilus · 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 Q5SI93
- Elsewhere: RCSB PDB 1V98 · PDBe 1V98 · UniProt Q5SI93
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