Research workbench
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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | Calcium homeostasis modulator protein 2 | protein | 263 | 60% helix, 2% strand | Q9HA72 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 420 | 0.63 | 0.77 | 54 | empty |
| 2 | 364 | 0.62 | 0.78 | 45 | empty |
| 3 | 395 | 0.62 | 0.77 | 49 | empty |
| 4 | 179 | 0.60 | 0.82 | 29 | empty |
| 5 | 173 | 0.59 | 0.82 | 30 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9HA72
- Elsewhere: RCSB PDB 6LMU · PDBe 6LMU · UniProt Q9HA72
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