Research workbench
SUGAR/H+ symporter STP10 in outward occluded conformation
Analyse SUGAR/H+ symporter STP10 in outward occluded conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7AAQ
- Type
- protein
- Length
- 487 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sugar transport protein 10
- UniProt
- Q9LT15
- Ligands
- BGC
- Pockets
- 4 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sugar transport protein 10 | protein | 487 | 79% helix, 0% strand | Q9LT15 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 4 copies · chains A
- ACT · Acetate ion · additive · 2 copies · chains A
- XPE · 3,6,9,12,15,18,21,24,27-nonaoxanonacosane-1,29-diol · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 603 | 0.87 | 0.92 | 84 | BGC, XPE, ACT |
| 2 | 102 | 0.68 | 0.91 | 26 | empty |
| 3 | 59 | 0.32 | 0.77 | 16 | empty |
| 4 | 69 | 0.31 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q9LT15
- Elsewhere: RCSB PDB 7AAQ · PDBe 7AAQ · UniProt Q9LT15
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.