Research workbench
Cryo-EM structure of human CALHM2 gap junction
Analyse Cryo-EM structure of human CALHM2 gap junction in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UIX
- Type
- protein
- Length
- 6,050 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 0.73
Structure
electron microscopy · 1 distinct chain · 70% 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 | 275 | 70% 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 | 1198 | 0.73 | 0.77 | 136 | empty |
| 2 | 574 | 0.71 | 0.79 | 81 | empty |
| 3 | 509 | 0.68 | 0.79 | 67 | empty |
| 4 | 490 | 0.68 | 0.79 | 66 | empty |
| 5 | 477 | 0.68 | 0.79 | 65 | empty |
Interfaces
55 interfaces between chains.
- G–H · 2799 Ų buried · 15 hydrogen bonds · protein-protein
- U–V · 2798 Ų buried · 15 hydrogen bonds · protein-protein
- M–N · 2798 Ų buried · 15 hydrogen bonds · protein-protein
- J–K · 2798 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 2797 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 44 disulfide (disulfide).
Compared structures
- 6UIX · Cryo-EM structure of human CALHM2 gap junction · the same entry in another collection · chain K against K, 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 6UIX · PDBe 6UIX · UniProt Q9HA72
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