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Cryo-EM structure of the human CALHM2

Analyse Cryo-EM structure of the human CALHM2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LMU
Type
protein
Length
2,893 residues
Chains
11
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.4
Source
Homo sapiens
Molecule
Calcium homeostasis modulator protein 2
UniProt
Q9HA72
Pockets
20 · best druggability 0.63

Structure

electron microscopy · resolution 3.4 · 1 distinct chain · 60% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KCalcium homeostasis modulator protein 2protein26360% helix, 2% strandQ9HA72

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14200.630.7754empty
23640.620.7845empty
33950.620.7749empty
41790.600.8229empty
51730.590.8230empty

Interfaces

22 interfaces between chains.

  • F–G · 2809 Ų buried · 23 hydrogen bonds · protein-protein
  • G–H · 2809 Ų buried · 23 hydrogen bonds · protein-protein
  • J–K · 2805 Ų buried · 23 hydrogen bonds · protein-protein
  • A–B · 2802 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 2802 Ų buried · 23 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 22 disulfide (disulfide).

Compared structures

  • 6LMU · Cryo-EM structure of the human CALHM2 · the same entry in another collection · chain K against K, TM-score 1.00
  • Q9HA72 · AlphaFold monomer V2.0 prediction for calcium homeostasis modulator protein 2 (Q9HA72) · a predicted model of the same protein · chain J against A, TM-score 0.89

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