Research workbench
D-dopachrome tautomerase
Analyse D-dopachrome tautomerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DPT
- Type
- protein
- Length
- 351 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- D-dopachrome tautomerase
- UniProt
- P30046
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | D-dopachrome tautomerase | protein | 117 | 40% helix, 28% strand | P30046 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 291 | 0.56 | 0.76 | 25 | empty |
| 2 | 106 | 0.39 | 0.76 | 22 | empty |
| 3 | 65 | 0.36 | 0.77 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–B · 291 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 203 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
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 P30046
- Elsewhere: RCSB PDB 1DPT · PDBe 1DPT · UniProt P30046
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.