Research workbench
N terminal domain of Mycobacterium avium complex Lon protease
Analyse N terminal domain of Mycobacterium avium complex Lon protease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IHG
- Type
- protein
- Length
- 186 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.397
- Source
- Mycobacterium [tuberculosis] TKK-01-0051
- Molecule
- Lon protease
- EC
- 3.4.21.53
- UniProt
- A0A051TYQ1
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · resolution 2.397 · 1 distinct chain · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lon protease (EC 3.4.21.53) | protein | 186 | 39% helix, 30% strand | A0A051TYQ1 |
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 | 111 | 0.37 | 0.74 | 22 | empty |
Compared structures
- 6IHG · N terminal domain of mycobacterium avium complex lon protease · 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 A0A051TYQ1
- Elsewhere: RCSB PDB 6IHG · PDBe 6IHG · UniProt A0A051TYQ1
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