Human GLUT1 in complex with inhibitor (2~{S})-3-(2-bromophenyl)-2-[2-(4-methoxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-phenylethyl]propanamide. Determined by X-ray diffraction at 2.99 Å resolution. Released 13 Apr 2016.
Explore 5EQH in 3D Show helices and sheets RCSB PDB PDBe
5EQH contains 26 α-helices and 0 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-31 | 22 | |
| α-helix | 37-52 | 16 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-90 | 33 | |
| α-helix | 93-98 | 6 | |
| α-helix | 100-111 | 12 | |
| α-helix | 119-145 | 27 | |
| α-helix | 150-156 | 7 | |
| α-helix | 159-173 | 15 | |
| α-helix | 186-191 | 6 | |
| α-helix | 194-203 | 10 | |
| α-helix | 204-206 | 3 | |
| α-helix | 208-210 | 3 | |
| α-helix | 211-215 | 5 | |
| α-helix | 221-231 | 11 | |
| α-helix | 238-251 | 14 | |
| α-helix | 259-264 | 6 | |
| α-helix | 269-283 | 15 | |
| α-helix | 288-300 | 13 | |
| α-helix | 306-328 | 23 | |
| α-helix | 333-356 | 24 | |
| α-helix | 364-379 | 16 | |
| α-helix | 388-391 | 4 | |
| α-helix | 400-429 | 30 | |
| α-helix | 430-432 | 3 | |
| α-helix | 433-450 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 2, facilitated glucose transporter member 1 | A | protein | 492 | Homo sapiens | P11166 (AlphaFold model) |
>5EQH_1 Solute carrier family 2, facilitated glucose transporter member 1 (chains A) MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTT LTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFE MLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIM GNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHD LQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEK AGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQ LPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGM CFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPE ELFHPLGADSQV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 5RF | (2~{S})-3-(2-bromophenyl)-2-[2-(4-methoxyphenyl)ethanoylamino]-~{N}-[(1~{S})-1-… | C26 H27 Br N2 O3 | 1 |
Mechanism of inhibition of human glucose transporter GLUT1 is conserved between cytochalasin B and phenylalanine amides. Kapoor, K., Finer-Moore, J.S., Pedersen, B.P. et al. Proc Natl Acad Sci U S A (2016) 113:4711-4716. DOI 10.1073/pnas.1603735113 · PubMed
Other PDB entries of the same protein (UniProt P11166 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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