Research workbench
Crystal structure of thermus aquaticus GFH1
Analyse Crystal structure of thermus aquaticus GFH1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ETN
- Type
- protein
- Length
- 464 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Anti-cleavage anti-grea transcription factor GFH1
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Anti-cleavage anti-grea transcription factor GFH1 | protein | 154 | 38% helix, 20% strand | — |
| B, C | Anti-cleavage anti-grea transcription factor GFH1 | protein | 155 | 36% helix, 25% strand | — |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 65 | 0.68 | 0.95 | 19 | empty |
| 2 | 143 | 0.38 | 0.73 | 19 | empty |
| 3 | 88 | 0.34 | 0.75 | 17 | empty |
| 4 | 55 | 0.31 | 0.77 | 17 | empty |
Interfaces
2 interfaces between chains.
- A–C · 1035 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 693 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2ETN · Crystal structure of Thermus aquaticus Gfh1 · 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 2ETN · PDBe 2ETN
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.