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Cryo-EM structure of the C. elegans clhm-1

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

PDB
6LMV
Type
protein
Length
2,223 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Calcium homeostasis modulator protein
UniProt
Q18593
Pockets
20 · best druggability 0.65

Structure

electron microscopy · 1 distinct chain · 69% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, ICalcium homeostasis modulator proteinprotein24769% helix, 1% strandQ18593

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14010.650.7834empty
24240.640.7839empty
33500.640.7929empty
44170.640.7836empty
54220.640.7735empty

Interfaces

18 interfaces between chains.

  • D–E · 2708 Ų buried · 19 hydrogen bonds · protein-protein
  • A–I · 2702 Ų buried · 19 hydrogen bonds · protein-protein
  • G–H · 2701 Ų buried · 19 hydrogen bonds · protein-protein
  • E–F · 2700 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 2698 Ų buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 27 disulfide (disulfide).

Compared structures

  • 6LMV · Cryo-EM structure of the C. elegans CLHM-1 · the same entry in another collection · chain I against I, TM-score 1.00
  • Q18593 · AlphaFold monomer V2.0 prediction for calcium homeostasis modulator protein (Q18593) · a predicted model of the same protein · chain C against A, TM-score 0.94

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