Research workbench
Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation
Analyse Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6THA
- Type
- protein
- Length
- 448 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute carrier family 2, facilitated glucose transporter member 1
- UniProt
- P11166
- Ligands
- BNG, CL
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 80% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Solute carrier family 2, facilitated glucose transporter member 1 | protein | 448 | 80% helix, 0% strand | P11166 |
Ligands and binding sites
- BNG · nonyl beta-D-glucopyranoside · ligand · 2 copies · chains A
- CL · Chloride ion · ion · chains A
- P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.78 | 0.79 | 84 | BNG, P33 |
| 2 | 54 | 0.35 | 0.78 | 12 | empty |
| 3 | 50 | 0.33 | 0.77 | 10 | empty |
| 4 | 55 | 0.28 | 0.74 | 16 | empty |
Compared structures
- 6THA · Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation · the same entry in another collection · chain A against A, TM-score 1.00
- P11166 · AlphaFold monomer V2.0 prediction for solute carrier family 2, facilitated glucose… · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P11166
- Elsewhere: RCSB PDB 6THA · PDBe 6THA · UniProt P11166
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