Research workbench
Human GLUT1 in complex with cytochalasin B
Analyse Human GLUT1 in complex with cytochalasin B in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EQI
- Type
- protein
- Length
- 447 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
- 5RH
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Solute carrier family 2, facilitated glucose transporter member 1 | protein | 447 | 75% helix, 0% strand | P11166 |
Ligands and binding sites
- 5RH · Cytochalasin B · ligand · 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 | 871 | 0.79 | 0.81 | 61 | 5RH |
| 2 | 142 | 0.44 | 0.76 | 27 | empty |
| 3 | 56 | 0.36 | 0.78 | 12 | empty |
| 4 | 53 | 0.36 | 0.79 | 11 | empty |
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 P11166
- Elsewhere: RCSB PDB 5EQI · PDBe 5EQI · UniProt P11166
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