Research workbench
Room temperature X-ray structure of perdeuterated PLL lectin
Analyse Room temperature X-ray structure of perdeuterated PLL lectin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B7E
- Type
- protein
- Length
- 354 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.6
- Source
- Photorhabdus laumondii
- Molecule
- PLL lectin
- UniProt
- A0A329WTS5
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · resolution 1.6 · 1 distinct chain · 0% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PLL lectin | protein | 354 | 0% helix, 47% strand | A0A329WTS5 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.79 | 0.82 | 47 | empty |
| 2 | 68 | 0.33 | 0.76 | 17 | empty |
Compared structures
- 7B7E · Room temperature X-ray structure of perdeuterated pll lectin · 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 A0A329WTS5
- Elsewhere: RCSB PDB 7B7E · PDBe 7B7E · UniProt A0A329WTS5
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