7UNL: Human TMEM175 in an open state

Human TMEM175 in an open state. Determined by electron microscopy at 2.45 Å resolution. Released 1 Jun 2022.

Method: Electron microscopy
Resolution: 2.45 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,824
Mol. weight: 111.65 kDa
Released: 1 Jun 2022

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

Secondary structure: helices and β-sheets

7UNL contains 46 α-helices and 12 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: 23 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	1
α-helix	34-48	15
α-helix	50-52	3
α-helix	53-56	4
α-helix	64-66	3
α-helix	67-101	35
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	170-172	3
β-strand	256	1	2
α-helix	258-283	26
α-helix	286-287	2
α-helix	290-293	4
α-helix	299-304	6
α-helix	307-331	25
β-strand	334	1	3
β-strand	337	1	2
α-helix	339-352	14
α-helix	355-361	7
α-helix	369-398	30
α-helix	401-404	4
β-strand	405	1	3
α-helix	407-409	3
α-helix	416-439	24
α-helix	441-460	20
α-helix	462-475	14

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

>7UNL_1 Endosomal/lysosomal potassium channel TMEM175 (chains A, B)
MSQPRTPEQALDTPGDCPPGRRDEDAGEGIQCSQRMLSFSDALLSIIATVMILPVTHTEI
SPEQQFDRSVQRLLATRIAVYLMTFLIVTVAWAAHTRLFQVVGKTDDTLALLNLACMMTI
TFLPYTFSLMVTFPDVPLGIFLFCVCVIAIGVVQALIVGYAFHFPHLLSPQIQRSAHRAL
YRRHVLGIVLQGPALCFAAAIFSLFFVPLSYLLMVTVILLPYVSKVTGWCRDRLLGHREP
SAHPVEVFSFDLHEPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVKERFSGSLV
AALSATGPRFLAYFGSFATVGLLWFAHHSLFLHVRKATRAMGLLNTLSLAFVGGLPLAYQ
QTSAFARQPRDELERVRVSCTIIFLASIFQLAMWTTALLHQAETLQPSVWFGGREHVLMF
AKLALYPCASLLAFASTCLLSRFSVGIFHLMQIAVPCAFLLLRLLVGLALATLRVLRGLA
RPEHPPPAPTGQDDPQSQLLPAPC

Primary citation

Differential ion dehydration energetics explains selectivity in the non-canonical lysosomal K + channel TMEM175. Oh, S., Marinelli, F., Zhou, W. et al. Elife (2022) 11. DOI 10.7554/eLife.75122 · PubMed

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

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
9VSP 3.4 Å, The DCY1020-bound structure of TMEM175

Browse structure collections

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