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Cryo-EM structure of the calcium homeostasis modulator 1 channel

Analyse Cryo-EM structure of the calcium homeostasis modulator 1 channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LYG
Type
protein
Length
1,856 residues
Chains
8
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Calcium homeostasis modulator 1
UniProt
E7F2J4
Ligands
NAG
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 70% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, HCalcium homeostasis modulator 1protein23270% helix, 1% strandE7F2J4

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H

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

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17310.750.8058empty
25390.750.8240empty
36780.750.8047empty
45450.750.8247empty
55420.750.8247empty

Interfaces

8 interfaces between chains.

  • A–B · 1823 Ų buried · 7 hydrogen bonds · protein-protein
  • F–G · 1823 Ų buried · 7 hydrogen bonds · protein-protein
  • D–E · 1822 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 1820 Ų buried · 7 hydrogen bonds · protein-protein
  • A–H · 1819 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 8 glycan (disulfide, N-glycosylation).

Compared structures

  • 6LYG · Cryo-EM structure of the calcium homeostasis modulator 1 channel · the same entry in another collection · chain A against A, TM-score 1.00

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