Research workbench
Crystal structure of the cytosolic domain of mouse MID51 bound to ADP
Analyse Crystal structure of the cytosolic domain of mouse MID51 bound to ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OAG
- Type
- protein
- Length
- 652 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial dynamic protein MID51
- UniProt
- Q8BGV8
- Ligands
- ADP, SO4
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial dynamic protein MID51 | protein | 328 | 47% helix, 18% strand | Q8BGV8 |
| B | Mitochondrial dynamic protein MID51 | protein | 324 | 48% helix, 19% strand | Q8BGV8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 852 | 0.75 | 0.79 | 92 | ADP, SO4 |
| 2 | 658 | 0.72 | 0.79 | 79 | ADP |
| 3 | 89 | 0.39 | 0.77 | 19 | empty |
| 4 | 67 | 0.36 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 1226 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 4OAG · Crystal structure of the cytosolic domain of mouse MiD51 bound to ADP · the same entry in another collection · chain A against A, TM-score 1.00
- Q8BGV8 · AlphaFold monomer V2.0 prediction for mitochondrial dynamics protein MID51 (Q8BGV8) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q8BGV8
- Elsewhere: RCSB PDB 4OAG · PDBe 4OAG · UniProt Q8BGV8
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