MolNFT v1 · #102055 · protein
Crystal structure of the cytosolic domain of mouse MID51 bound to ADP
4OAG · Mitochondrial dynamic protein MID51: “Crystal structure of the cytosolic domain of mouse MID51 bound to ADP”. X-ray diffraction, 2 ligands (ADP, SO4), 4 pockets (best druggability 0.75). MolNFT v1 #102055 on GenesisL1: 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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