Research workbench
Bdlp-like folding of mitofusin 1
Analyse Bdlp-like folding of mitofusin 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GNT
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitofusin-1
- EC
- 3.6.5.-
- UniProt
- Q8IWA4
- Ligands
- GDP
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitofusin-1 (EC 3.6.5.-) | protein | 378 | 56% helix, 12% strand | Q8IWA4 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.57 | 0.83 | 26 | GDP |
| 2 | 62 | 0.27 | 0.72 | 16 | empty |
| 3 | 54 | 0.26 | 0.74 | 13 | empty |
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 Q8IWA4
- Elsewhere: RCSB PDB 5GNT · PDBe 5GNT · UniProt Q8IWA4
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