HsPepT2 bound to Ala-Phe in the inward facing partially occluded conformation. Determined by electron microscopy at 3.8 Å resolution. Released 20 Oct 2021.
Explore 7PMY in 3D Show helices and sheets RCSB PDB PDBe
7PMY contains 35 α-helices and 23 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 | 42-45 | 4 | |
| α-helix | 47-65 | 19 | |
| α-helix | 67-69 | 3 | |
| α-helix | 70-74 | 5 | |
| α-helix | 79-94 | 16 | |
| α-helix | 97-107 | 11 | |
| α-helix | 110-131 | 22 | |
| α-helix | 134-136 | 3 | |
| α-helix | 139-170 | 32 | |
| α-helix | 177-207 | 31 | |
| α-helix | 217-237 | 21 | |
| α-helix | 238-240 | 3 | |
| α-helix | 244-247 | 4 | |
| α-helix | 250-269 | 20 | |
| α-helix | 276-278 | 3 | |
| α-helix | 280-284 | 5 | |
| α-helix | 290-303 | 14 | |
| α-helix | 304-306 | 3 | |
| α-helix | 310-316 | 7 | |
| α-helix | 319-323 | 5 | |
| α-helix | 324-327 | 4 | |
| β-strand | 331 | 1 | 1 |
| α-helix | 338-340 | 3 | |
| α-helix | 342-346 | 5 | |
| α-helix | 347-358 | 12 | |
| α-helix | 359-363 | 5 | |
| α-helix | 364-370 | 7 | |
| α-helix | 372-374 | 3 | |
| α-helix | 378-404 | 27 | |
| α-helix | 405-407 | 3 | |
| β-strand | 410 | 1 | 2 |
| β-strand | 413-420 | 8 | 2 |
| β-strand | 426-431 | 6 | 3 |
| β-strand | 437-443 | 7 | 3 |
| β-strand | 447-448 | 2 | 2 |
| β-strand | 453-456 | 4 | 2 |
| β-strand | 461-470 | 10 | 3 |
| β-strand | 473-482 | 10 | 3 |
| β-strand | 486-494 | 9 | 2 |
| β-strand | 497-505 | 9 | 2 |
| β-strand | 516-521 | 6 | 4 |
| β-strand | 527-530 | 4 | 5 |
| β-strand | 537-539 | 3 | 5 |
| β-strand | 544-545 | 2 | 4 |
| α-helix | 546-548 | 3 | |
| β-strand | 549-550 | 2 | 4 |
| β-strand | 554-555 | 2 | 6 |
| β-strand | 559-563 | 5 | 5 |
| β-strand | 567-570 | 4 | 5 |
| β-strand | 574-575 | 2 | 6 |
| β-strand | 580-588 | 9 | 4 |
| β-strand | 592-601 | 10 | 4 |
| β-strand | 607 | 1 | 1 |
| α-helix | 608-611 | 4 | |
| α-helix | 612-636 | 25 | |
| α-helix | 638 | 1 | |
| α-helix | 642-666 | 25 | |
| α-helix | 671-694 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Solute carrier family 15 member 2 | A | protein | 729 | Homo sapiens | Q16348 (AlphaFold model) |
| Ala-phe | B | protein | 2 | Homo sapiens |
>7PMY_1 Solute carrier family 15 member 2 (chains A) MNPFQKNESKETLFSPVSIEEVPPRPPSPPKKPSPTICGSNYPLSIAFIVVNEFCERFSY YGMKAVLILYFLYFLHWNEDTSTSIYHAFSSLCYFTPILGAAIADSWLGKFKTIIYLSLV YVLGHVIKSLGALPILGGQVVHTVLSLIGLSLIALGTGGIKPCVAAFGGDQFEEKHAEER TRYFSVFYLSINAGSLISTFITPMLRGDVQCFGEDCYALAFGVPGLLMVIALVVFAMGSK IYNKPPPEGNIVAQVFKCIWFAISNRFKNRSGDIPKRQHWLDWAAEKYPKQLIMDVKALT RVLFLYIPLPMFWALLDQQGSRWTLQAIRMNRNLGFFVLQPDQMQVLNPLLVLIFIPLFD FVIYRLVSKCGINFSSLRKMAVGMILACLAFAVAAAVEIKINEMAPAQPGPQEVFLQVLN LADDEVKVTVVGNENNSLLIESIKSFQKTPHYSKLHLKTKSQDFHFHLKYHNLSLYTEHS VQEKNWYSLVIREDGNSISSMMVKDTESRTTNGMTTVRFVNTLHKDVNISLSTDTSLNVG EDYGVSAYRTVQRGEYPAVHCRTEDKNFSLNLGLLDFGAAYLFVITNNTNQGLQAWKIED IPANKMSIAWQLPQYALVTAGEVMFSVTGLEFSYSQAPSSMKSVLQAAWLLTIAVGNIIV LVVAQFSGLVQWAEFILFSCLLLVICLIFSIMGYYYVPVKTEDMRGPADKHIPHIQGNMI KLETKKTKL
>7PMY_2 ALA-PHE (chains B) AF
Structural snapshots of human PepT1 and PepT2 reveal mechanistic insights into substrate and drug transport across epithelial membranes. Killer, M., Wald, J., Pieprzyk, J. et al. Sci Adv (2021) 7:eabk3259-eabk3259. DOI 10.1126/sciadv.abk3259 · PubMed
Other PDB entries of the same protein (UniProt Q16348 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 7PMY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.