Research workbench
Lar controls the expression of the listeria monocytogenes agr system and mediates virulence.
Analyse Lar controls the expression of the listeria monocytogenes agr system and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EP3
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LMO0651 protein
- UniProt
- Q8Y982
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LMO0651 protein | protein | 215 | 73% helix, 2% strand | Q8Y982 |
| B | LMO0651 protein | protein | 218 | 74% helix, 4% strand | Q8Y982 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 10 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 948 | 0.77 | 0.79 | 74 | empty |
| 2 | 462 | 0.60 | 0.75 | 45 | EDO |
| 3 | 52 | 0.38 | 0.81 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1160 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6EP3 · Lar controls the expression of the Listeria monocytogenes agr system and mediates… · 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 Q8Y982
- Elsewhere: RCSB PDB 6EP3 · PDBe 6EP3 · UniProt Q8Y982
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