Research workbench
Crystal structure of ABC sugar transporter (periplasmic sugar binding protein) from legionella pneumophila
Analyse Crystal structure of ABC sugar transporter (periplasmic sugar binding protein)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ROT
- Type
- protein
- Length
- 545 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC sugar transporter, periplasmic sugar binding protein
- UniProt
- Q5ZZ27
- Pockets
- 8 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC sugar transporter, periplasmic sugar binding protein | protein | 273 | 47% helix, 17% strand | Q5ZZ27 |
| B | ABC sugar transporter, periplasmic sugar binding protein | protein | 272 | 46% helix, 17% strand | Q5ZZ27 |
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
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 428 | 0.79 | 0.88 | 46 | empty |
| 2 | 58 | 0.70 | 0.97 | 18 | GOL |
| 3 | 113 | 0.53 | 0.82 | 23 | empty |
| 4 | 96 | 0.49 | 0.82 | 22 | empty |
| 5 | 62 | 0.34 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1239 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 3ROT · Crystal structure of ABC sugar transporter (periplasmic sugar binding protein) from… · 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 Q5ZZ27
- Elsewhere: RCSB PDB 3ROT · PDBe 3ROT · UniProt Q5ZZ27
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