Research workbench
Structure of legionella effector LEGA15
Analyse Structure of legionella effector LEGA15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KJ6
- Type
- protein
- Length
- 884 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ankyrin repeat-containing protein
- UniProt
- Q5ZSR1
- Ligands
- CL
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ankyrin repeat-containing protein | protein | 443 | 58% helix, 9% strand | Q5ZSR1 |
| B | Ankyrin repeat-containing protein | protein | 441 | 58% helix, 9% strand | Q5ZSR1 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1030 | 0.81 | 0.82 | 73 | PEG |
| 2 | 274 | 0.55 | 0.77 | 32 | TRS |
| 3 | 179 | 0.54 | 0.79 | 23 | PEG |
| 4 | 179 | 0.54 | 0.79 | 36 | PEG |
| 5 | 91 | 0.49 | 0.82 | 20 | PEG |
Interfaces
1 interface between chains.
- A–B · 663 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 7KJ6 · Structure of Legionella Effector LegA15 · 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 Q5ZSR1
- Elsewhere: RCSB PDB 7KJ6 · PDBe 7KJ6 · UniProt Q5ZSR1
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