Research workbench
Crystal structure of human GLUT3 bound to D-glucose in the outward- occluded conformation at 1.5 ångström
Analyse Crystal structure of human GLUT3 bound to D-glucose in the outward- occluded… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ZW9
- Type
- protein
- Length
- 470 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Solute carrier family 2, facilitated glucose transporter member 3
- UniProt
- P11169
- Ligands
- GLC, BGC
- Pockets
- 4 · best druggability 0.79
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 3 | protein | 470 | 80% helix, 0% strand | P11169 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 3 copies · 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 | 511 | 0.79 | 0.85 | 60 | OLC, GLC, BGC |
| 2 | 91 | 0.36 | 0.75 | 21 | empty |
| 3 | 55 | 0.33 | 0.76 | 11 | empty |
| 4 | 63 | 0.30 | 0.74 | 12 | empty |
Compared structures
- 4ZW9 · Crystal structure of human GLUT3 bound to D-glucose in the outward-occluded conformation… · the same entry in another collection · chain A against A, TM-score 1.00
- P11169 · 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 0.98
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 P11169
- Elsewhere: RCSB PDB 4ZW9 · PDBe 4ZW9 · UniProt P11169
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