Research workbench
Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q
Analyse Crystal structure of the Lon-like protease MtaLonC with S582A mutation in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EV4
- Type
- protein
- Length
- 596 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.12
- Source
- Meiothermus taiwanensis; SYNTHETIC CONSTRUCT
- Molecule
- Endopeptidase La; F-b20-Q peptide {ortho-aminobenzoic acid (Abz)…
- EC
- 3.4.21.53
- UniProt
- C9DRU9
- Ligands
- PO4
- Pockets
- 7 · best druggability 0.61
Structure
x-ray diffraction · resolution 2.12 · 2 distinct chains · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endopeptidase La (EC 3.4.21.53) | protein | 592 | 40% helix, 20% strand | C9DRU9 |
| S | F-b20-Q peptide {ortho-aminobenzoic acid (Abz)- QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A} | protein | 4 | 0% helix, 50% 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
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 337 | 0.61 | 0.78 | 23 | empty |
| 2 | 152 | 0.57 | 0.83 | 17 | empty |
| 3 | 154 | 0.57 | 0.82 | 19 | empty |
| 4 | 81 | 0.55 | 0.85 | 21 | empty |
| 5 | 65 | 0.36 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–S · 459 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 7EV4 · Crystal structure of the lon-like protease mtalonc with S582A 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 7EV4 · PDBe 7EV4 · UniProt C9DRU9
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