Research workbench
Cryo-EM structure of a dimer of undecameric human CALHM2
Analyse Cryo-EM structure of a dimer of undecameric human CALHM2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VAI
- Type
- protein
- Length
- 5,874 residues
- Chains
- 22
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium homeostasis modulator protein 2
- UniProt
- Q9HA72
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 64% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V | Calcium homeostasis modulator protein 2 | protein | 267 | 64% 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 | 1174 | 0.80 | 0.81 | 112 | empty |
| 2 | 961 | 0.76 | 0.78 | 87 | empty |
| 3 | 758 | 0.75 | 0.80 | 67 | empty |
| 4 | 868 | 0.74 | 0.78 | 62 | empty |
| 5 | 837 | 0.74 | 0.79 | 64 | empty |
Interfaces
66 interfaces between chains.
- Q–R · 2809 Ų buried · 14 hydrogen bonds · protein-protein
- A–K · 2790 Ų buried · 15 hydrogen bonds · protein-protein
- H–I · 2786 Ų buried · 15 hydrogen bonds · protein-protein
- N–O · 2783 Ų buried · 15 hydrogen bonds · protein-protein
- E–F · 2783 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 disulfide (disulfide).
Compared structures
- 6VAI · Cryo-EM structure of a dimer of undecameric human CALHM2 · the same entry in another collection · chain I against I, TM-score 1.00
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 6VAI · PDBe 6VAI · UniProt Q9HA72
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