Research workbench
Crystal structure of the Lon-like protease MtaLonC with D582A mutation in complex with substrate polypeptide
Analyse Crystal structure of the Lon-like protease MtaLonC with D582A mutation in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EUY
- Type
- protein
- Length
- 592 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Meiothermus taiwanensis; SYNTHETIC CONSTRUCT
- Molecule
- Endopeptidase La; Ala-pro-glu-ala-val
- EC
- 3.4.21.53
- UniProt
- C9DRU9
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endopeptidase La (EC 3.4.21.53) | protein | 587 | 41% helix, 21% strand | C9DRU9 |
| S | Ala-pro-glu-ala-val | protein | 5 | 0% helix, 40% strand | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 314 | 0.60 | 0.78 | 29 | empty |
| 2 | 97 | 0.56 | 0.85 | 20 | empty |
| 3 | 159 | 0.56 | 0.82 | 16 | empty |
| 4 | 121 | 0.53 | 0.81 | 19 | empty |
| 5 | 72 | 0.39 | 0.79 | 22 | empty |
Interfaces
1 interface between chains.
- A–S · 489 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7EUY · Crystal structure of the lon-like protease mtalonc with D582A mutation in complex with… · 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 C9DRU9
- Elsewhere: RCSB PDB 7EUY · PDBe 7EUY · UniProt C9DRU9
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