Research workbench
Crystal structure of ABC transporter alpha-glycoside-binding mutant protein W287A in complex with trehalose
Analyse Crystal structure of ABC transporter alpha-glycoside-binding mutant protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JB0
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.63
- Source
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- Molecule
- ABC transporter, periplasmic substrate-binding protein
- UniProt
- Q5SLD7
- Ligands
- GLC
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · resolution 1.63 · 1 distinct chain · 49% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ABC transporter, periplasmic substrate-binding protein | protein | 404 | 49% helix, 16% strand | Q5SLD7 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · chains A
- CIT · Citric acid · additive · chains A
- GOL · Glycerol · additive · chains A
- PDO · 1,3-propandiol · additive · chains A
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 | 213 | 0.82 | 0.96 | 36 | GLC, EDO |
| 2 | 55 | 0.33 | 0.77 | 19 | empty |
Compared structures
- 6JB0 · Crystal structure of ABC transporter alpha-glycoside-binding mutant protein W287A in… · 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 Q5SLD7
- Elsewhere: RCSB PDB 6JB0 · PDBe 6JB0 · UniProt Q5SLD7
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