Research workbench
CALHM1 open state with disordered cth
Analyse CALHM1 open state with disordered cth in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DSC
- Type
- protein
- Length
- 1,528 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calcium homeostasis modulator 1
- UniProt
- E7F2J4
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Calcium homeostasis modulator 1 | protein | 191 | 67% helix, 1% strand | E7F2J4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1076 | 0.75 | 0.77 | 89 | empty |
| 2 | 998 | 0.75 | 0.77 | 68 | empty |
| 3 | 1170 | 0.75 | 0.77 | 96 | empty |
| 4 | 970 | 0.74 | 0.77 | 81 | empty |
| 5 | 836 | 0.74 | 0.78 | 60 | empty |
Interfaces
8 interfaces between chains.
- B–C · 1247 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1246 Ų buried · 9 hydrogen bonds · protein-protein
- G–H · 1242 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 1242 Ų buried · 9 hydrogen bonds · protein-protein
- E–F · 1240 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
- 7DSC · CALHM1 open state with disordered CTH · the same entry in another collection · chain A against A, 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 E7F2J4
- Elsewhere: RCSB PDB 7DSC · PDBe 7DSC · UniProt E7F2J4
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