Research workbench
Cryo-EM structure of human CALHM2
Analyse Cryo-EM structure of human CALHM2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VAK
- Type
- protein
- Length
- 2,992 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium homeostasis modulator protein 2
- UniProt
- Q9HA72
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 68% helix, 1% 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 | 272 | 68% helix, 1% 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 | 971 | 0.75 | 0.78 | 89 | empty |
| 2 | 979 | 0.75 | 0.77 | 90 | empty |
| 3 | 1035 | 0.75 | 0.77 | 102 | empty |
| 4 | 498 | 0.67 | 0.78 | 42 | empty |
| 5 | 524 | 0.66 | 0.77 | 48 | empty |
Interfaces
22 interfaces between chains.
- F–G · 2792 Ų buried · 18 hydrogen bonds · protein-protein
- I–J · 2788 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 2756 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 2752 Ų buried · 14 hydrogen bonds · protein-protein
- J–K · 2749 Ų buried · 16 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 6VAK · PDBe 6VAK · UniProt Q9HA72
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