7V5D: Mouse ABCB9

Cryo-EM structure of the mouse ABCB9 (PG-bound). Determined by electron microscopy at 3.4 Å resolution. Released 19 Oct 2022.

Method
Electron microscopy
Resolution
3.4 Å
Organism
Mus musculus
Chains
2
Atoms
8,822
Mol. weight
168.84 kDa
Ligands
PGT
Released
19 Oct 2022

Explore 7V5D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 30 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix171-1755
α-helix178-1803
α-helix181-21333
α-helix220-2267
α-helix227-2337
α-helix234-26330
α-helix271-2755
α-helix280-2834
α-helix284-2885
α-helix289-2946
α-helix295-3006
α-helix301-32020
α-helix322-36847
α-helix371-3755
α-helix381-43252
α-helix438-47134
α-helix473-4797
α-helix481-4833
β-strand500-50341
β-strand522-52431
β-strand52612
β-strand52912
β-strand531-53333
α-helix544-5485
β-strand560-56121
β-strand564-56521
α-helix566-5683
α-helix571-5777
β-strand57814
β-strand59115
α-helix595-5973
α-helix605-6139
α-helix619-6224
β-strand63115
α-helix633-6364
α-helix641-65111
β-strand659-66024
β-strand66316
α-helix673-6786
β-strand689-69024
β-strand691-69223
β-strand69316
α-helix699-7013
β-strand706-70723
β-strand708-71037
β-strand713-71647
α-helix720-7256
α-helix733-7364
Chain B: 27 helices, 12 β-strands
ElementResiduesLengthSheet
α-helix170-1734
α-helix178-1803
α-helix181-21333
α-helix220-2267
α-helix227-2337
α-helix234-26330
α-helix271-2755
α-helix280-29415
α-helix295-2995
α-helix300-32021
α-helix322-36948
α-helix371-3777
α-helix381-43353
α-helix438-47134
α-helix475-4784
β-strand49118
β-strand500-50459
β-strand505-507310
β-strand518-521410
β-strand531-534411
α-helix542-5487
β-strand556-56169
β-strand56519
β-strand56918
α-helix571-5777
α-helix592-5954
α-helix605-6139
α-helix618-6214
α-helix633-6364
α-helix641-65313
β-strand659-663511
α-helix673-6775
α-helix678-6825
β-strand689-693511
α-helix697-6993
β-strand707-710411
β-strand713-716411
α-helix720-7256
α-helix731-7377

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ABC-type oligopeptide transporter ABCB9A, Bprotein762Mus musculusQ9JJ59 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7V5D_1 ABC-type oligopeptide transporter ABCB9 (chains A, B)
MRLWKAVVVTLAFVSTDVGVTTAIYAFSHLDRSLLEDIRHFNIFDSVLDLWAACLYRSCL
LLGATIGVAKNSALGPRRLRASWLVITLVCLFVGIYAMAKLLLFSEVRRPIRDPWFWALF
VWTYISLAASFLLWGLLATVRPDAEALEPGNEGFHGEGGAPAEQASGATLQKLLSYTKPD
VAFLVAASFFLIVAALGETFLPYYTGRAIDSIVIQKSMDQFTTAVVVVCLLAIGSSLAAG
IRGGIFTLVFARLNIRLRNCLFRSLVSQETSFFDENRTGDLISRLTSDTTMVSDLVSQNI
NIFLRNTVKVTGVVVFMFSLSWQLSLVTFMGFPIIMMVSNIYGKYYKRLSKEVQSALARA
STTAEETISAMKTVRSFANEEEEAEVFLRKLQQVYKLNRKEAAAYMSYVWGSGLTLLVVQ
VSILYYGGHLVISGQMSSGNLIAFIIYEFVLGDCMESVGSVYSGLMQGVGAAEKVFEFID
RQPTMVHDGSLAPDHLEGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSG
KSSCVNILENFYPLQGGRVLLDGKPIGAYDHKYLHRVISLVSQEPVLFARSITDNISYGL
PTVPFEMVVEAAQKANAHGFIMELQDGYSTETGEKGAQLSGGQKQRVAMARALVRNPPVL
ILDEATSALDAESEYLIQQAIHGNLQRHTVLIIAHRLSTVERAHLIVVLDKGRVVQQGTH
QQLLAQGGLYAKLVQRQMLGLEHPLDYTASHKEPPSNTEHKA

Ligands and cofactors

IDNameFormulaCopies
PGT(1S)-2-{[{[(2R)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(palmitoylo…C40 H79 O10 P1

Primary citation

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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