Research workbench
Cryo-EM structure of a dimer of decameric human CALHM4 in the presence of CA2+
Analyse Cryo-EM structure of a dimer of decameric human CALHM4 in the presence of CA2+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6YTO
- Type
- protein
- Length
- 5,340 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium homeostasis modulator protein 4
- UniProt
- Q5JW98
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 72% helix, 0% 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 | Calcium homeostasis modulator protein 4 | protein | 267 | 72% helix, 0% strand | Q5JW98 |
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 | 1077 | 0.79 | 0.81 | 91 | empty |
| 2 | 885 | 0.78 | 0.80 | 96 | empty |
| 3 | 882 | 0.78 | 0.80 | 78 | empty |
| 4 | 848 | 0.77 | 0.80 | 81 | empty |
| 5 | 547 | 0.73 | 0.81 | 61 | empty |
Interfaces
50 interfaces between chains.
- F–G · 2123 Ų buried · 7 hydrogen bonds · protein-protein
- N–O · 2123 Ų buried · 6 hydrogen bonds · protein-protein
- Q–R · 2070 Ų buried · 5 hydrogen bonds · protein-protein
- G–H · 2066 Ų buried · 7 hydrogen bonds · protein-protein
- R–S · 2060 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 40 disulfide (disulfide).
Compared structures
- 6YTO · Cryo-EM structure of a dimer of decameric human CALHM4 in the presence of Ca2+ · 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 Q5JW98
- Elsewhere: RCSB PDB 6YTO · PDBe 6YTO · UniProt Q5JW98
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