MolNFT v1 · #48326 · protein
Crystal structure of thioredoxin-2
2PPT: “Crystal structure of thioredoxin-2”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.44). MolNFT v1 #48326 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2PPT
- Type
- protein
- Length
- 292 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Thioredoxin-2
- EC
- 1.8.1.8
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.44
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-2 (EC 1.8.1.8) | protein | 149 | 30% helix, 29% strand | — |
| B | Thioredoxin-2 (EC 1.8.1.8) | protein | 143 | 30% helix, 28% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.44 | 0.84 | 19 | empty |
| 2 | 50 | 0.41 | 0.83 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 545 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2PPT · Crystal structure of thioredoxin-2 · 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
- Elsewhere: RCSB PDB 2PPT · PDBe 2PPT
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