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Structure of an apo membrane protein

Analyse Structure of an apo membrane protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W8O
Type: protein
Length: 832 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ENDOSOMAL/LYSOSOMAL potassium channel TMEM175
UniProt: Q9BSA9
Pockets: 18 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 76% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	ENDOSOMAL/LYSOSOMAL potassium channel TMEM175	protein	416	76% helix, 0% strand	Q9BSA9

Pockets

18 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	585	0.80	0.85	74	empty
2	502	0.79	0.86	62	empty
3	615	0.75	0.82	89	empty
4	278	0.60	0.79	50	empty
5	122	0.53	0.82	32	empty

Interfaces

1 interface between chains.

A–B · 3011 Å² buried · 15 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6W8O · Structure of an Apo membrane protein · the same entry in another collection · chain B against B, TM-score 1.00
Q9BSA9 · AlphaFold monomer V2.0 prediction for ENDOSOMAL/LYSOSOMAL potassium channel TMEM175… · a predicted model of the same protein · chain A against A, TM-score 0.88

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9BSA9
Elsewhere: RCSB PDB 6W8O · PDBe 6W8O · UniProt Q9BSA9

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