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Designed pentameric channel qlll

Analyse Designed pentameric channel qlll in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7UDY
Type
protein
Length
378 residues
Chains
15
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Designed channel qlll
Pockets
9 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ADesigned channel qlllprotein2492% helix, 0% strand—
B, D, L, NDesigned channel qlllprotein2688% helix, 0% strand—
C, E, F, G, H, I, J, K, M, ODesigned channel qlllprotein2592% helix, 0% strand—

Ligands and binding sites

  • C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 3 copies · chains B, C, D, A, G, N, O

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12130.800.9236empty
23550.790.8840C8E
31930.790.9235empty
41100.740.9325empty
52910.730.8530empty

Interfaces

27 interfaces between chains.

  • N–O · 618 Ų buried · 2 hydrogen bonds · protein-protein
  • F–G · 612 Ų buried · 1 hydrogen bond · protein-protein
  • K–O · 609 Ų buried · 0 hydrogen bonds · protein-protein
  • F–J · 599 Ų buried · 0 hydrogen bonds · protein-protein
  • K–L · 596 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7UDY · Designed pentameric channel QLLL · the same entry in another collection · chain C against C, TM-score 1.00

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