7LF6: Lysosomal membrane protein

Name: PDB 7LF6: Structure of lysosomal membrane protein
Published: 2022-01-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: membrane protein

Structure of lysosomal membrane protein. Determined by electron microscopy at 3.5 Å resolution. Released 26 Jan 2022.

Method: Electron microscopy
Resolution: 3.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 6,288
Mol. weight: 111.33 kDa
Released: 26 Jan 2022

Explore 7LF6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7LF6 contains 36 α-helices and 4 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.

Chains A and B: 18 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	36-49	14
α-helix	52-56	5
α-helix	67-101	35
α-helix	107-132	26
α-helix	137-163	27
α-helix	181-205	25
α-helix	212-222	11
α-helix	254-257	4
α-helix	258-283	26
α-helix	286-287	2
α-helix	293-295	3
α-helix	299-332	34
β-strand	334	1	1
α-helix	339-352	14
α-helix	355-363	9
α-helix	373-395	23
β-strand	405	1	1
α-helix	407-409	3
α-helix	416-436	21
α-helix	445-468	24

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

>7LF6_1 Endosomal/lysosomal potassium channel TMEM175 (chains A, B)
MSQPRTPEQALDTPGDCPPGRRDEDAGEGIQCSQRMLSFSDALLSIIATVMILPVTHTEI
SPEQQFDRSVQRLLATRIAVYLMTFLIVTVAWAAHTRLFQVVGKTDDTLALLNLACMMTI
TFLPYTFSLMVTFPDVPLGIFLFCVCVIAIGVVQALIVGYAFHFPHLLSPQIQRSAHRAL
YRRHVLGIVLQGPALCFAAAIFSLFFVPLSYLLMVTVILLPYVSKVTGWCRDRLLGHREP
SAHPVEVFSFDLHEPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVKERFSGSLV
AALSATGPRFLAYFGSFATVGLLWFAHHSLFLHVRKATRAMGLLNTLSLAFVGGLPLAYQ
QTSAFARQPRDELERVRVSCTIIFLASIFQLAMWTTALLHQAETLQPSVWFGGREHVLMF
AKLALYPCASLLAFASTCLLSRFSVGIFHLMQIAVPCAFLLLRLLVGLALATLRVLRGLA
RPEHPPPAPTGQDDPQSQLLPAPC

Primary citation

pH regulates potassium conductance and drives a constitutive proton current in human TMEM175. Zheng, W., Shen, C., Wang, L. et al. Sci Adv (2022) 8:eabm1568-eabm1568. DOI 10.1126/sciadv.abm1568 · 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

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