7V5C: Mouse ABCB9

Cryo-EM structure of the mouse ABCB9 (ADP.BeF3-bound). Determined by electron microscopy at 3.2 Å resolution. Released 19 Oct 2022.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Mus musculus
Chains: 2
Atoms: 8,916
Mol. weight: 169.13 kDa
Ligands: MG, BEF, ADP
Released: 19 Oct 2022

Explore 7V5C in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7V5C contains 62 α-helices and 29 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, 14 β-strands

Element	Residues	Length	Sheet
α-helix	170-175	6
α-helix	181-214	34
α-helix	217-220	4
α-helix	222-265	44
α-helix	270-273	4
α-helix	278-283	6
α-helix	284-288	5
α-helix	289-318	30
α-helix	325-328	4
α-helix	332-338	7
α-helix	345-357	13
α-helix	385-400	16
α-helix	402-431	30
α-helix	437-454	18
α-helix	461-471	11
α-helix	475-478	4
α-helix	481-483	3
β-strand	500-507	8	1
β-strand	518-525	8	1
β-strand	531-533	3	2
β-strand	534	1	3
α-helix	542-544	3
β-strand	558-561	4	1
β-strand	564-565	2	1
α-helix	566-568	3
α-helix	571-574	4
β-strand	578-581	4	2
β-strand	591	1	4
α-helix	605-610	6
α-helix	618-621	4
α-helix	627-629	3
β-strand	631	1	4
α-helix	633-636	4
α-helix	646-653	8
β-strand	659-662	4	2
α-helix	666-669	4
α-helix	674-681	8
β-strand	691-693	3	2
α-helix	697-701	5
β-strand	705	1	2
β-strand	707-710	4	3
β-strand	713-717	5	3
α-helix	720-724	5
α-helix	734-737	4

Chain B: 32 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	170-173	4
α-helix	181-214	34
α-helix	221-243	23
α-helix	249-265	17
α-helix	270-273	4
α-helix	280-283	4
α-helix	284-288	5
α-helix	289-302	14
α-helix	306-314	9
α-helix	316-319	4
α-helix	325-328	4
α-helix	332-341	10
α-helix	345-358	14
α-helix	385-395	11
α-helix	399-429	31
α-helix	430-434	5
α-helix	439-454	16
α-helix	461-471	11
α-helix	475-478	4
α-helix	481-483	3
β-strand	500-506	7	5
β-strand	519-524	6	5
β-strand	531-533	3	6
β-strand	534	1	7
α-helix	542-544	3
β-strand	558-561	4	5
β-strand	564-565	2	5
α-helix	566-568	3
α-helix	571-574	4
β-strand	578-581	4	6
β-strand	591	1	8
α-helix	605-610	6
α-helix	618-621	4
α-helix	627-629	3
β-strand	631	1	8
α-helix	633-636	4
α-helix	643-653	11
β-strand	659-662	4	6
α-helix	674-682	9
β-strand	689	1	6
β-strand	691-693	3	6
β-strand	705	1	6
β-strand	707-709	3	7
β-strand	714-717	4	7
α-helix	720-724	5
α-helix	730-733	4
α-helix	734-737	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ABC-type oligopeptide transporter ABCB9	A, B	protein	762	Mus musculus	Q9JJ59 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7V5C_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

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
BEF	Beryllium trifluoride ion	Be F3	2
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2

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:

7V5D 3.4 Å, Cryo-EM structure of the mouse ABCB9 (PG-bound)
7VFI 3.98 Å, Cryo-EM structure of the mouse TAPL (9mer-peptide bound)

Browse structure collections

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