6WCC: Human closed state TMEM175 in CsCl

Human closed state TMEM175 in CsCl. Determined by electron microscopy at 3.24 Å resolution. Released 15 Apr 2020.

Method: Electron microscopy
Resolution: 3.24 Å
Organism: Homo sapiens
Chains: 2
Atoms: 5,721
Mol. weight: 112 kDa
Ligands: CS
Released: 15 Apr 2020

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

Secondary structure: helices and β-sheets

6WCC contains 42 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: 21 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	1
α-helix	34-49	16
α-helix	50-52	3
α-helix	53-56	4
α-helix	68-102	35
β-strand	105	1	1
α-helix	107-121	15
α-helix	123-132	10
α-helix	138-163	26
α-helix	165-167	3
α-helix	255-257	3
α-helix	258-283	26
α-helix	286-287	2
α-helix	288-294	7
α-helix	299-332	34
α-helix	339-352	14
α-helix	355-358	4
α-helix	372-399	28
α-helix	401-404	4
α-helix	407-409	3
α-helix	416-439	24
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

>6WCC_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
CS	Cesium ion	Cs	5

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
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
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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