Research workbench
Flavin-dependent Tryptophan 6-halogenase Thal
Analyse Flavin-dependent Tryptophan 6-halogenase Thal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H43
- Type
- protein
- Length
- 1,049 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Streptomyces albogriseolus
- Molecule
- Tryptophan 6-halogenase Thal
- UniProt
- A1E280
- Ligands
- K, PO4
- Pockets
- 13 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tryptophan 6-halogenase Thal | protein | 528 | 40% helix, 20% strand | A1E280 |
| B | Tryptophan 6-halogenase Thal | protein | 521 | 38% helix, 21% strand | A1E280 |
Ligands and binding sites
- K · Potassium ion · metal · chains A
- PO4 · Phosphate ion · ion · 6 copies · chains A, B
- GOL · Glycerol · additive · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.81 | 0.82 | 103 | GOL |
| 2 | 754 | 0.76 | 0.81 | 70 | GOL |
| 3 | 786 | 0.76 | 0.80 | 68 | GOL |
| 4 | 159 | 0.64 | 0.85 | 36 | empty |
| 5 | 80 | 0.56 | 0.87 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 2008 Ų buried · 37 hydrogen bonds · protein-protein
Compared structures
- 6H43 · Flavin-dependent tryptophan 6-halogenase thal · 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 A1E280
- Elsewhere: RCSB PDB 6H43 · PDBe 6H43 · UniProt A1E280
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