Research workbench
3.7 angstrom cryoEM structure of full length human TRPM4
Analyse 3.7 angstrom cryoEM structure of full length human TRPM4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BWI
- Type
- protein
- Length
- 3,264 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.7
- Source
- Homo sapiens
- Molecule
- Transient receptor potential cation channel subfamily M member 4
- Ligands
- Y01, NAG, NA
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · resolution 3.7 · 1 distinct chain · 55% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transient receptor potential cation channel subfamily M member 4 | protein | 816 | 55% helix, 1% strand | — |
Ligands and binding sites
- Y01 · Cholesterol hemisuccinate · ligand · 24 copies · chains A, B, D, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
- NA · Sodium ion · metal · 5 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 519 | 0.86 | 0.92 | 39 | NA |
| 2 | 478 | 0.78 | 0.86 | 63 | empty |
| 3 | 483 | 0.78 | 0.86 | 64 | empty |
| 4 | 528 | 0.77 | 0.84 | 79 | empty |
| 5 | 746 | 0.77 | 0.82 | 92 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2854 Ų buried · 16 hydrogen bonds · protein-protein
- A–D · 2851 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 2833 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 2831 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 98 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 1 covalent, 1 glycan (disulfide, covalent ligand, N-glycosylation).
Compared structures
- 6BWI · 3.7 ångström cryoem structure of full length human TRPM4 · 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
- Elsewhere: RCSB PDB 6BWI · PDBe 6BWI
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