8VIC: AP-6 bound human TMEM175

AP-6 bound human TMEM175. Determined by electron microscopy at 3.48 Å resolution. Released 14 Aug 2024.

Method: Electron microscopy
Resolution: 3.48 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,562
Mol. weight: 111.6 kDa
Ligands: A1AA3
Released: 14 Aug 2024

Explore 8VIC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8VIC contains 45 α-helices and 8 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: 23 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	1
α-helix	34-48	15
α-helix	49-51	3
α-helix	52-57	6
α-helix	68-101	34
β-strand	105	1	1
α-helix	107-120	14
α-helix	123-132	10
α-helix	137-163	27
α-helix	165-167	3
α-helix	255-257	3
α-helix	258-273	16
α-helix	275-283	9
α-helix	286-287	2
α-helix	288-294	7
α-helix	299-305	7
α-helix	307-332	26
β-strand	334	1	2
α-helix	339-352	14
α-helix	355-363	9
α-helix	369-399	31
α-helix	401-403	3
β-strand	405	1	2
α-helix	407-409	3
α-helix	416-439	24
α-helix	444-460	17
α-helix	462-472	11

Chain B: 22 helices, 4 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	3
α-helix	34-48	15
α-helix	52-56	5
α-helix	68-101	34
β-strand	105	1	3
α-helix	107-120	14
α-helix	123-132	10
α-helix	137-163	27
α-helix	165-167	3
α-helix	255-257	3
α-helix	258-273	16
α-helix	275-283	9
α-helix	286-287	2
α-helix	288-294	7
α-helix	299-305	7
α-helix	307-330	24
β-strand	334	1	4
α-helix	339-352	14
α-helix	355-363	9
α-helix	369-399	31
α-helix	401-403	3
β-strand	405	1	4
α-helix	407-409	3
α-helix	416-439	24
α-helix	444-460	17
α-helix	462-472	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Endosomal/lysosomal potassium channel TMEM175	A, B	protein	504	Homo sapiens	Q9BSA9 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8VIC_1 Endosomal/lysosomal potassium channel TMEM175 (chains A, B)
MSQPRTPEQALDTPGDCPPGRRDEDAGEGIQCSQRMLSFSDALLSIIATVMILPVTHTEI
SPEQQFDRSVQRLLATRIAVYLMTFLIVTVAWAAHTRLFQVVGKTDDTLALLNLACMMTI
TFLPYTFSLMVTFPDVPLGIFLFCVCVIAIGVVQALIVGYAFHFPHLLSPQIQRSAHRAL
YRRHVLGIVLQGPALCFAAAIFSLFFVPLSYLLMVTVILLPYVSKVTGWCRDRLLGHREP
SAHPVEVFSFDLHEPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVKERFSGSLV
AALSATGPRFLAYFGSFATVGLLWFAHHSLFLHVRKATRAMGLLNTLSLAFVGGLPLAYQ
QTSAFARQPRDELERVRVSCTIIFLASIFQLAMWTTALLHQAETLQPSVWFGGREHVLMF
AKLALYPCASLLAFASTCLLSRFSVGIFHLMQIAVPCAFLLLRLLVGLALATLRVLRGLA
RPEHPPPAPTGQDDPQSQLLPAPC

Ligands and cofactors

ID	Name	Formula	Copies
A1AA3	(2P,2'P)-2,2'-(1,3-phenylene)di(pyridin-4-amine)	C16 H14 N4	1

Primary citation

Discovery of Selective Inhibitors for the Lysosomal Parkinson's Disease Channel TMEM175. Oh, S., Lee, J., Choi, H.J. et al. J Am Chem Soc (2024) 146:23230-23239. DOI 10.1021/jacs.4c05623 · PubMed

Other PDB entries of the same protein (UniProt Q9BSA9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7UNL 2.45 Å, Human TMEM175 in an open state
7UNM 2.61 Å, Human TMEM175 in an closed state
6WC9 2.64 Å, Human open state TMEM175 in KCl
8DHM 2.73 Å, Human TMEM175 in complex with 4-aminopyridine
9VSQ 2.74 Å, The TUG-891-bound structure of TMEM175
9VSR 2.92 Å, The DCY1040 and TUG-891-bound structure of TMEM175
6WCA 3.03 Å, Human closed state TMEM175 in KCl
6WCB 3.17 Å, Human open state TMEM175 in CsCl
6W8N 3.2 Å, Structure of a trans-membrane protein
6WCC 3.24 Å, Human closed state TMEM175 in CsCl
6W8O 3.4 Å, Structure of an Apo membrane protein
8FYF 3.4 Å, Human TMEM175-LAMP1 transmembrane domain only complex

Browse structure collections

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