Research workbench
Crystal structure of the cytosolic domain of human CNNM3
Analyse Crystal structure of the cytosolic domain of human CNNM3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6MN6
- Type
- protein
- Length
- 590 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.36
- Source
- Homo sapiens
- Molecule
- Metal transporter CNNM3
- UniProt
- Q8NE01
- Pockets
- 7 · best druggability 0.77
Structure
x-ray diffraction · resolution 3.36 · 2 distinct chains · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metal transporter CNNM3 | protein | 293 | 31% helix, 26% strand | Q8NE01 |
| B | Metal transporter CNNM3 | protein | 297 | 31% helix, 27% strand | Q8NE01 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 94 | 0.77 | 0.97 | 22 | empty |
| 2 | 132 | 0.61 | 0.85 | 23 | empty |
| 3 | 240 | 0.58 | 0.79 | 26 | empty |
| 4 | 71 | 0.49 | 0.84 | 13 | empty |
| 5 | 148 | 0.47 | 0.77 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 3594 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
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 Q8NE01
- Elsewhere: RCSB PDB 6MN6 · PDBe 6MN6 · UniProt Q8NE01
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.