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Crystal structure of the potassium channel MTTMEM175 with cesium

Analyse Crystal structure of the potassium channel MTTMEM175 with cesium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6HDA
Type
protein
Length
693 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NANOBODY,MALTOSE/MALTODEXTRIN-binding periplasmic protein; TMEM175
UniProt
P0AEX9, E4TN31
Ligands
GLC, CS
Pockets
7 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANANOBODY,MALTOSE/MALTODEXTRIN-binding periplasmic proteinprotein46136% helix, 23% strandP0AEX9
BTMEM175protein23275% helix, 0% strandE4TN31

Ligands and binding sites

  • GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
  • CS · Cesium ion · metal
  • LMT · Dodecyl-beta-D-maltoside · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12690.700.8530GLC
24590.670.7838empty
32010.500.7636empty
4960.480.8118empty
51090.380.7521LMT

Interfaces

1 interface between chains.

  • A–B · 534 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 6HDA · Crystal structure of the potassium channel MtTMEM175 with cesium · the same entry in another collection · chain A against A, TM-score 1.00
  • E4TN31 · AlphaFold monomer V2.0 prediction for potassium channel FTRAC_2467 (E4TN31) · a predicted model of the same protein · chain B against A, TM-score 0.89

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