Research workbench
CALHM1 close state with ordered cth
Analyse CALHM1 close state with ordered cth in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DSE
- Type
- protein
- Length
- 1,631 residues
- Chains
- 7
- 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 · 71% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Calcium homeostasis modulator 1 | protein | 233 | 71% helix, 1% strand | E7F2J4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A, B, C, D, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 990 | 0.75 | 0.77 | 65 | empty |
| 2 | 968 | 0.75 | 0.78 | 62 | empty |
| 3 | 743 | 0.74 | 0.79 | 47 | empty |
| 4 | 901 | 0.74 | 0.77 | 56 | empty |
| 5 | 756 | 0.74 | 0.79 | 49 | empty |
Interfaces
14 interfaces between chains.
- E–F · 1958 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1956 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1954 Ų buried · 8 hydrogen bonds · protein-protein
- F–G · 1954 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 1951 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 7 glycan (disulfide, N-glycosylation).
Compared structures
- 7DSE · CALHM1 close state with ordered 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 7DSE · PDBe 7DSE · UniProt E7F2J4
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