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Cryo-EM structure of an undecameric chicken CALHM1 and human CALHM2 chimera

Analyse Cryo-EM structure of an undecameric chicken CALHM1 and human CALHM2 chimera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VAL
Type
protein
Length
2,827 residues
Chains
11
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Green fluorescent protein, CALHM1,CALMH2 chimera
UniProt
P42212, A0A1D5NWS1, Q9HA72
Pockets
20 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 67% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KGreen fluorescent protein, CALHM1,CALMH2 chimeraprotein25767% helix, 0% strandP42212, A0A1D5NWS1, Q9HA72

Pockets

20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15320.710.8078empty
25360.710.8083empty
34990.700.8076empty
44800.700.8071empty
54110.690.8166empty

Interfaces

22 interfaces between chains.

  • A–K · 2771 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 2769 Ų buried · 21 hydrogen bonds · protein-protein
  • I–J · 2768 Ų buried · 20 hydrogen bonds · protein-protein
  • B–C · 2767 Ų buried · 20 hydrogen bonds · protein-protein
  • J–K · 2765 Ų buried · 20 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 disulfide (disulfide).

Compared structures

  • 6VAL · Cryo-EM structure of an undecameric chicken CALHM1 and human CALHM2 chimera · 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 E against A, TM-score 0.90

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