Research workbench
Truncated mitofusin-1, transition-like state
Analyse Truncated mitofusin-1, transition-like state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GOM
- Type
- protein
- Length
- 811 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitofusin-1
- EC
- 3.6.5.-
- UniProt
- Q8IWA4
- Ligands
- GDP
- Pockets
- 7 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 58% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitofusin-1 (EC 3.6.5.-) | protein | 407 | 57% helix, 12% strand | Q8IWA4 |
| B | Mitofusin-1 (EC 3.6.5.-) | protein | 404 | 59% helix, 11% strand | Q8IWA4 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- DTT · 2,3-dihydroxy-1,4-dithiobutane · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1054 | 0.82 | 0.83 | 118 | GDP |
| 2 | 126 | 0.43 | 0.77 | 19 | empty |
| 3 | 82 | 0.36 | 0.76 | 17 | empty |
| 4 | 65 | 0.31 | 0.75 | 17 | empty |
| 5 | 83 | 0.30 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1122 Ų buried · 17 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 Q8IWA4
- Elsewhere: RCSB PDB 5GOM · PDBe 5GOM · UniProt Q8IWA4
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