Cryo-EM structure of the mouse TAPL (9mer-peptide bound). Determined by electron microscopy at 3.98 Å resolution. Released 19 Oct 2022.
Explore 7VFI in 3D Show helices and sheets RCSB PDB PDBe
7VFI contains 50 α-helices and 34 β-strands across 2 chains. 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 | 171-175 | 5 | |
| α-helix | 178-180 | 3 | |
| α-helix | 181-213 | 33 | |
| α-helix | 219-226 | 8 | |
| α-helix | 227-233 | 7 | |
| α-helix | 234-265 | 32 | |
| α-helix | 270-275 | 6 | |
| α-helix | 278-294 | 17 | |
| α-helix | 295-299 | 5 | |
| α-helix | 300-320 | 21 | |
| α-helix | 322-369 | 48 | |
| α-helix | 371-375 | 5 | |
| α-helix | 380-432 | 53 | |
| α-helix | 438-479 | 42 | |
| α-helix | 481-483 | 3 | |
| β-strand | 500-501 | 2 | 1 |
| β-strand | 505 | 1 | 2 |
| β-strand | 521 | 1 | 2 |
| β-strand | 524-525 | 2 | 1 |
| β-strand | 531-533 | 3 | 3 |
| α-helix | 544-547 | 4 | |
| β-strand | 560-561 | 2 | 1 |
| β-strand | 564-565 | 2 | 1 |
| α-helix | 571-577 | 7 | |
| β-strand | 578 | 1 | 4 |
| β-strand | 591 | 1 | 5 |
| α-helix | 592-596 | 5 | |
| α-helix | 605-615 | 11 | |
| α-helix | 618-622 | 5 | |
| α-helix | 627-629 | 3 | |
| β-strand | 631 | 1 | 5 |
| α-helix | 633-636 | 4 | |
| α-helix | 641-653 | 13 | |
| β-strand | 659 | 1 | 4 |
| β-strand | 661-663 | 3 | 3 |
| α-helix | 673-677 | 5 | |
| α-helix | 678-682 | 5 | |
| β-strand | 691-693 | 3 | 3 |
| β-strand | 705-707 | 3 | 3 |
| β-strand | 708-710 | 3 | 6 |
| β-strand | 713-716 | 4 | 6 |
| α-helix | 720-725 | 6 | |
| α-helix | 731-736 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 171-177 | 7 | |
| α-helix | 178-180 | 3 | |
| α-helix | 181-213 | 33 | |
| α-helix | 218-266 | 49 | |
| α-helix | 270-275 | 6 | |
| α-helix | 279-294 | 16 | |
| α-helix | 295-299 | 5 | |
| α-helix | 300-320 | 21 | |
| α-helix | 322-369 | 48 | |
| α-helix | 371-377 | 7 | |
| α-helix | 380-432 | 53 | |
| α-helix | 438-472 | 35 | |
| β-strand | 491 | 1 | 7 |
| β-strand | 500 | 1 | 8 |
| β-strand | 503-504 | 2 | 9 |
| β-strand | 505-508 | 4 | 10 |
| β-strand | 516-521 | 6 | 10 |
| β-strand | 530-532 | 3 | 11 |
| β-strand | 533 | 1 | 12 |
| α-helix | 543-548 | 6 | |
| β-strand | 556-558 | 3 | 9 |
| β-strand | 560-561 | 2 | 8 |
| β-strand | 564-565 | 2 | 8 |
| β-strand | 569 | 1 | 7 |
| α-helix | 571-577 | 7 | |
| β-strand | 591 | 1 | 13 |
| α-helix | 592-596 | 5 | |
| α-helix | 605-614 | 10 | |
| α-helix | 620-623 | 4 | |
| β-strand | 631 | 1 | 13 |
| α-helix | 641-653 | 13 | |
| β-strand | 659-663 | 5 | 11 |
| α-helix | 673-677 | 5 | |
| α-helix | 678-682 | 5 | |
| β-strand | 689-693 | 5 | 11 |
| α-helix | 697-699 | 3 | |
| β-strand | 707 | 1 | 12 |
| β-strand | 708-709 | 2 | 14 |
| β-strand | 714-716 | 3 | 14 |
| α-helix | 720-725 | 6 | |
| α-helix | 731-737 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ABC-type oligopeptide transporter ABCB9 | A, B | protein | 762 | Mus musculus | Q9JJ59 (AlphaFold model) |
| Arg-arg-tyr-gln-lys-ser-thr-glu-leu | C | protein | 9 | Mus musculus | P68433 (AlphaFold model) |
>7VFI_1 ABC-type oligopeptide transporter ABCB9 (chains A, B) MRLWKAVVVTLAFVSTDVGVTTAIYAFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCL LLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMAKLLLFSEVRRPIRDPWFWALF VWTYISLAASFLLWGLLATVRPDAEALEPGNEGFHGEGGAPAEQASGATLQKLLSYTKPD VAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAG IRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI NIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARA STTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQ VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFID RQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSG KSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL ILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTH QQLLAQGGLYAKLVQRQMLGLEHPLDYTASHKEPPSNTEHKA
>7VFI_2 ARG-ARG-TYR-GLN-LYS-SER-THR-GLU-LEU (chains C) RRYQKSTEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 3 |
The lysosomal transporter TAPL has a dual role as peptide translocator and phosphatidylserine floppase. Park, J.G., Kim, S., Jang, E. et al. Nat Commun (2022) 13:5851-5851. DOI 10.1038/s41467-022-33593-2 · PubMed
Other PDB entries of the same protein (UniProt Q9JJ59 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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