6WC9: Human open state TMEM175 in KCl

Human open state TMEM175 in KCl. Determined by electron microscopy at 2.64 Å resolution. Released 15 Apr 2020.

Method: Electron microscopy
Resolution: 2.64 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,809
Mol. weight: 111.61 kDa
Released: 15 Apr 2020

Explore 6WC9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WC9 contains 44 α-helices and 16 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: 22 helices, 8 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	67-101	35
β-strand	102	1	2
β-strand	105	1	1
α-helix	107-120	14
α-helix	123-132	10
α-helix	138-163	26
α-helix	165-167	3
β-strand	168	1	2
α-helix	170-172	3
α-helix	255	1
β-strand	256	1	3
α-helix	257	1
α-helix	258-283	26
α-helix	288-294	7
α-helix	299-305	7
α-helix	307-331	25
β-strand	334	1	4
β-strand	337	1	3
α-helix	339-352	14
α-helix	355-363	9
α-helix	369-398	30
β-strand	405	1	4
α-helix	407-409	3
α-helix	416-438	23
α-helix	444-460	17
α-helix	462-507	14

Chain B: 22 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	5
α-helix	34-48	15
α-helix	50-52	3
α-helix	53-56	4
α-helix	67-101	35
β-strand	102	1	6
β-strand	105	1	5
α-helix	107-120	14
α-helix	123-132	10
α-helix	138-163	26
α-helix	165-167	3
β-strand	168	1	6
α-helix	170-172	3
α-helix	255	1
β-strand	256	1	7
α-helix	257	1
α-helix	258-283	26
α-helix	288-294	7
α-helix	299-305	7
α-helix	307-331	25
β-strand	334	1	8
β-strand	337	1	7
α-helix	339-352	14
α-helix	355-363	9
α-helix	369-398	30
β-strand	405	1	8
α-helix	407-409	3
α-helix	416-438	23
α-helix	444-460	17
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

>6WC9_1 Endosomal/lysosomal potassium channel TMEM175 (chains A, B)
MSQPRTPEQALDTPGDCPPGRRDEDAGEGIQCSQRMLSFSDALLSIIATVMILPVTHTEI
SPEQQFDRSVQRLLATRIAVYLMTFLIVTVAWAAHTRLFQVVGKTDDTLALLNLACMMTI
TFLPYTFSLMVTFPDVPLGIFLFCVCVIAIGVVQALIVGYAFHFPHLLSPQIQRSAHRAL
YRRHVLGIVLQGPALCFAAAIFSLFFVPLSYLLMVTVILLPYVSKVTGWCRDRLLGHREP
SAHPVEVFSFDLHEPLSKERVEAFSDGVYAIVATLLILDICEDNVPDPKDVKERFSGSLV
AALSATGPRFLAYFGSFATVGLLWFAHHSLFLHVRKATRAMGLLNTLSLAFVGGLPLAYQ
QTSAFARQPRDELERVRVSCTIIFLASIFQLAMWTTALLHQAETLQPSVWFGGREHVLMF
AKLALYPCASLLAFASTCLLSRFSVGIFHLMQIAVPCAFLLLRLLVGLALATLRVLRGLA
RPEHPPPAPTGQDDPQSQLLPAPC

Primary citation

Gating and selectivity mechanisms for the lysosomal K + channel TMEM175. Oh, S., Paknejad, N., Hite, R.K. Elife (2020) 9. DOI 10.7554/eLife.53430 · 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
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

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