Research workbench
Crystal structure of ABC transporter alpha-glycoside-binding mutant protein R356A in complex with maltose
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
- 6JAN
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, periplasmic substrate-binding protein
- UniProt
- Q5SLD7
- Ligands
- GLC
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 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 · 5 copies · chains A
- CIT · Citric acid · additive · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.80 | 0.97 | 34 | GLC |
| 2 | 57 | 0.47 | 0.84 | 14 | EDO |
| 3 | 60 | 0.36 | 0.78 | 18 | empty |
| 4 | 54 | 0.32 | 0.77 | 20 | empty |
Compared structures
- 6JAN · Crystal structure of ABC transporter alpha-glycoside-binding mutant protein R356A 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 6JAN · PDBe 6JAN · UniProt Q5SLD7
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