Crystal structure of human sugar transporter GLUT1 (SLC2A1) in the inward conformation. Determined by X-ray diffraction at 2.4 Å resolution. Released 25 Nov 2020.
Explore 6THA in 3D Show helices and sheets RCSB PDB PDBe
6THA contains 30 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 | 11-31 | 21 | |
| α-helix | 37-52 | 16 | |
| α-helix | 55-57 | 3 | |
| α-helix | 58-81 | 24 | |
| α-helix | 83-90 | 8 | |
| α-helix | 92-111 | 20 | |
| α-helix | 113-116 | 4 | |
| α-helix | 119-147 | 29 | |
| α-helix | 153-157 | 5 | |
| 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 | 211-212 | 2 | |
| α-helix | 213-217 | 5 | |
| α-helix | 221-231 | 11 | |
| α-helix | 238-252 | 15 | |
| α-helix | 259-264 | 6 | |
| α-helix | 266-283 | 18 | |
| α-helix | 287-300 | 14 | |
| α-helix | 306-327 | 22 | |
| α-helix | 328-330 | 3 | |
| α-helix | 333-356 | 24 | |
| α-helix | 364-381 | 18 | |
| α-helix | 386-394 | 9 | |
| α-helix | 400-429 | 30 | |
| α-helix | 430-432 | 3 | |
| α-helix | 433-450 | 18 | |
| α-helix | 452-454 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 2, facilitated glucose transporter member 1 | A | protein | 496 | Homo sapiens | P11166 (AlphaFold model) |
>6THA_1 Solute carrier family 2, facilitated glucose transporter member 1 (chains A) MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTT LTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFE MLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIM GNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHD LQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEK AGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQ LPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGM CFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPE ELFHPLGADSQVLVPR
| ID | Name | Formula | Copies |
|---|---|---|---|
| BNG | nonyl beta-D-glucopyranoside | C15 H30 O6 | 2 |
| P33 | 3,6,9,12,15,18-hexaoxaicosane-1,20-diol | C14 H30 O8 | 1 |
Water and common crystallization additives (CL) are not listed.
Structural comparison of GLUT1 to GLUT3 reveal transport regulation mechanism in sugar porter family. Custodio, T.F., Paulsen, P.A., Frain, K.M. et al. Life Sci Alliance (2021) 4. DOI 10.26508/lsa.202000858 · 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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