Research workbench
Crystal structure of SlpA domain II (aa 201-310), domain that is involved in the self-assembly and dimerization of the S-layer from Lactobacillus acidophilus
Analyse Crystal structure of SlpA domain II (aa 201-310), domain that is involved in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8BT9
- Type
- protein
- Length
- 334 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Lactobacillus acidophilus
- Molecule
- S-layer protein
- UniProt
- P35829
- Ligands
- NCA
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · resolution 2.1 · 3 distinct chains · 21% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | S-layer protein | protein | 110 | 20% helix, 42% strand | P35829 |
| C | S-layer protein | protein | 109 | 20% helix, 43% strand | P35829 |
| B | S-layer protein | protein | 115 | 22% helix, 40% strand | P35829 |
Ligands and binding sites
- NCA · Nicotinamide · ligand · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 215 | 0.57 | 0.79 | 33 | NCA |
| 2 | 102 | 0.42 | 0.78 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–C · 527 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 483 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- P35829 · AlphaFold monomer V2.0 prediction for S-layer protein (P35829) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P35829
- Elsewhere: RCSB PDB 8BT9 · PDBe 8BT9 · UniProt P35829
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