Research workbench
Crystal structure of the periplasmic aliphatic sulphonate binding protein ssua from escherichia COLI
Analyse Crystal structure of the periplasmic aliphatic sulphonate binding protein ssua… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2X26
- Type
- protein
- Length
- 599 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Periplasmic aliphatic sulphonates-binding protein
- UniProt
- P75853
- Pockets
- 6 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Periplasmic aliphatic sulphonates-binding protein | protein | 308 | 44% helix, 18% strand | P75853 |
| B | Periplasmic aliphatic sulphonates-binding protein | protein | 291 | 49% helix, 19% strand | P75853 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.83 | 0.97 | 32 | GOL |
| 2 | 1019 | 0.78 | 0.80 | 86 | GOL |
| 3 | 64 | 0.33 | 0.76 | 17 | empty |
| 4 | 51 | 0.31 | 0.76 | 14 | empty |
| 5 | 53 | 0.29 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 105 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2X26 · Crystal structure of the periplasmic aliphatic sulphonate binding protein SsuA from… · the same entry in another collection · chain A against A, TM-score 1.00
- P75853 · AlphaFold monomer V2.0 prediction for putative aliphatic sulfonates- binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.91
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 P75853
- Elsewhere: RCSB PDB 2X26 · PDBe 2X26 · UniProt P75853
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