Research workbench
Fructo-oligosaccharide transporter bt 1762-63
Analyse Fructo-oligosaccharide transporter bt 1762-63 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ZAZ
- Type
- protein
- Length
- 1,476 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Susd homolog; Susc homolog
- UniProt
- Q8A6W4, Q8A6W3
- Ligands
- FRU, MG, CL
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Susd homolog | protein | 555 | 44% helix, 9% strand | Q8A6W4 |
| B | Susc homolog | protein | 921 | 11% helix, 47% strand | Q8A6W3 |
Ligands and binding sites
- FRU · beta-D-fructofuranose · sugar · 11 copies · chains B, A
- MG · Magnesium ion · metal · 2 copies · chains A, B
- CL · Chloride ion · ion · chains A, B
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.83 | 0.96 | 42 | empty |
| 2 | 625 | 0.79 | 0.85 | 89 | empty |
| 3 | 73 | 0.73 | 0.98 | 30 | empty |
| 4 | 503 | 0.69 | 0.80 | 55 | empty |
| 5 | 99 | 0.68 | 0.92 | 32 | empty |
Interfaces
1 interface between chains.
- A–B · 4100 Ų buried · 68 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6ZAZ · Fructo-oligosaccharide transporter BT 1762-63 · the same entry in another collection · chain B against B, 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 Q8A6W4
- Every structure of UniProt Q8A6W3
- Elsewhere: RCSB PDB 6ZAZ · PDBe 6ZAZ · UniProt Q8A6W4 · UniProt Q8A6W3
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