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Cryo-EM structure of human glucose transporter GLUT4 bound to cytochalasin B in lipid nanodiscs
Analyse Cryo-EM structure of human glucose transporter GLUT4 bound to cytochalasin B in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7WSM
- Type
- protein
- Length
- 464 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute carrier family 2, facilitated glucose transporter member 4
- UniProt
- P14672
- Ligands
- 5RH, NAG
- Pockets
- 5 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Solute carrier family 2, facilitated glucose transporter member 4 | protein | 464 | 78% helix, 0% strand | P14672 |
Ligands and binding sites
- 5RH · Cytochalasin B · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1031 | 0.79 | 0.81 | 73 | 5RH |
| 2 | 137 | 0.54 | 0.81 | 18 | empty |
| 3 | 135 | 0.44 | 0.76 | 19 | empty |
| 4 | 112 | 0.41 | 0.76 | 20 | empty |
| 5 | 53 | 0.28 | 0.74 | 15 | empty |
Modifications
Observed in the structure: 1 glycan (N-glycosylation).
Compared structures
- 7WSM · Cryo-EM structure of human glucose transporter GLUT4 bound to cytochalasin B in lipid… · the same entry in another collection · chain A against A, TM-score 1.00
- P14672 · 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 0.87
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 P14672
- Elsewhere: RCSB PDB 7WSM · PDBe 7WSM · UniProt P14672
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