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sugar/H+ symporter STP6 in inward occluded conformation with glucose bound

Analyse sugar/H+ symporter STP6 in inward occluded conformation with glucose bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 9G11
Type: protein
Length: 476 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.2
Source: Arabidopsis thaliana
Molecule: Sugar transport protein 6
UniProt: Q9SFG0
Ligands: Y01, BGC
Pockets: 3 · best druggability 0.82

Structure

x-ray diffraction · resolution 3.2 · 1 distinct chain · 77% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Sugar transport protein 6	protein	476	77% helix, 0% strand	Q9SFG0

Ligands and binding sites

Y01 · Cholesterol hemisuccinate · ligand · 3 copies · chains A
BGC · beta-D-glucopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	152	0.82	0.97	24	BGC
2	874	0.76	0.79	77	empty
3	55	0.31	0.76	17	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

Q9SFG0 · AlphaFold monomer V2.0 prediction for sugar transport protein 6 (Q9SFG0) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 Q9SFG0
Elsewhere: RCSB PDB 9G11 · PDBe 9G11 · UniProt Q9SFG0

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