Research workbench
Plant growth-promoting factor yxal from bacillus velezensis
Analyse Plant growth-promoting factor yxal from bacillus velezensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DXN
- Type
- protein
- Length
- 738 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Membrane associated protein kinase with beta-propeller domain, pyrrolo-quinoline quinone…
- UniProt
- A0A6H2JLK6
- Ligands
- CL
- Pockets
- 1 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Membrane associated protein kinase with beta-propeller domain, pyrrolo-quinoline quinone beta-propeller repeat | protein | 370 | 2% helix, 48% strand | A0A6H2JLK6 |
| B | Membrane associated protein kinase with beta-propeller domain, pyrrolo-quinoline quinone beta-propeller repeat | protein | 368 | 2% helix, 49% strand | A0A6H2JLK6 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1025 | 0.83 | 0.84 | 85 | CL |
Interfaces
1 interface between chains.
- A–B · 524 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 7DXN · Plant growth-promoting factor YxaL from Bacillus velezensis · 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 A0A6H2JLK6
- Elsewhere: RCSB PDB 7DXN · PDBe 7DXN · UniProt A0A6H2JLK6
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