Cryo-EM structure of the mouse ABCB9 (PG-bound). Determined by electron microscopy at 3.4 Å resolution. Released 19 Oct 2022.
Explore 7V5D in 3D Show helices and sheets RCSB PDB PDBe
7V5D contains 57 α-helices and 30 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 | 220-226 | 7 | |
| α-helix | 227-233 | 7 | |
| α-helix | 234-263 | 30 | |
| α-helix | 271-275 | 5 | |
| α-helix | 280-283 | 4 | |
| α-helix | 284-288 | 5 | |
| α-helix | 289-294 | 6 | |
| α-helix | 295-300 | 6 | |
| α-helix | 301-320 | 20 | |
| α-helix | 322-368 | 47 | |
| α-helix | 371-375 | 5 | |
| α-helix | 381-432 | 52 | |
| α-helix | 438-471 | 34 | |
| α-helix | 473-479 | 7 | |
| α-helix | 481-483 | 3 | |
| β-strand | 500-503 | 4 | 1 |
| β-strand | 522-524 | 3 | 1 |
| β-strand | 526 | 1 | 2 |
| β-strand | 529 | 1 | 2 |
| β-strand | 531-533 | 3 | 3 |
| α-helix | 544-548 | 5 | |
| β-strand | 560-561 | 2 | 1 |
| β-strand | 564-565 | 2 | 1 |
| α-helix | 566-568 | 3 | |
| α-helix | 571-577 | 7 | |
| β-strand | 578 | 1 | 4 |
| β-strand | 591 | 1 | 5 |
| α-helix | 595-597 | 3 | |
| α-helix | 605-613 | 9 | |
| α-helix | 619-622 | 4 | |
| β-strand | 631 | 1 | 5 |
| α-helix | 633-636 | 4 | |
| α-helix | 641-651 | 11 | |
| β-strand | 659-660 | 2 | 4 |
| β-strand | 663 | 1 | 6 |
| α-helix | 673-678 | 6 | |
| β-strand | 689-690 | 2 | 4 |
| β-strand | 691-692 | 2 | 3 |
| β-strand | 693 | 1 | 6 |
| α-helix | 699-701 | 3 | |
| β-strand | 706-707 | 2 | 3 |
| β-strand | 708-710 | 3 | 7 |
| β-strand | 713-716 | 4 | 7 |
| α-helix | 720-725 | 6 | |
| α-helix | 733-736 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 170-173 | 4 | |
| α-helix | 178-180 | 3 | |
| α-helix | 181-213 | 33 | |
| α-helix | 220-226 | 7 | |
| α-helix | 227-233 | 7 | |
| α-helix | 234-263 | 30 | |
| α-helix | 271-275 | 5 | |
| α-helix | 280-294 | 15 | |
| α-helix | 295-299 | 5 | |
| α-helix | 300-320 | 21 | |
| α-helix | 322-369 | 48 | |
| α-helix | 371-377 | 7 | |
| α-helix | 381-433 | 53 | |
| α-helix | 438-471 | 34 | |
| α-helix | 475-478 | 4 | |
| β-strand | 491 | 1 | 8 |
| β-strand | 500-504 | 5 | 9 |
| β-strand | 505-507 | 3 | 10 |
| β-strand | 518-521 | 4 | 10 |
| β-strand | 531-534 | 4 | 11 |
| α-helix | 542-548 | 7 | |
| β-strand | 556-561 | 6 | 9 |
| β-strand | 565 | 1 | 9 |
| β-strand | 569 | 1 | 8 |
| α-helix | 571-577 | 7 | |
| α-helix | 592-595 | 4 | |
| α-helix | 605-613 | 9 | |
| α-helix | 618-621 | 4 | |
| α-helix | 633-636 | 4 | |
| 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 | 707-710 | 4 | 11 |
| β-strand | 713-716 | 4 | 11 |
| 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) |
>7V5D_1 ABC-type oligopeptide transporter ABCB9 (chains A, B) MRLWKAVVVTLAFVSTDVGVTTAIYAFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCL LLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMAKLLLFSEVRRPIRDPWFWALF VWTYISLAASFLLWGLLATVRPDAEALEPGNEGFHGEGGAPAEQASGATLQKLLSYTKPD VAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAG IRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI NIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARA STTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQ VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFID RQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSG KSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL ILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTH QQLLAQGGLYAKLVQRQMLGLEHPLDYTASHKEPPSNTEHKA
| ID | Name | Formula | Copies |
|---|---|---|---|
| PGT | (1S)-2-{[{[(2R)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo… | C40 H79 O10 P | 1 |
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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