Research workbench
Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable coenzyme Q biosynthes
Analyse Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PED
- Type
- protein
- Length
- 387 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone activity of BC1 complex-like, mitochondrial
- EC
- 2.7.11.-
- UniProt
- Q8NI60
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone activity of BC1 complex-like, mitochondrial (EC 2.7.11.-) | protein | 387 | 57% helix, 13% strand | Q8NI60 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · 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 | 203 | 0.64 | 0.84 | 46 | empty |
| 2 | 76 | 0.45 | 0.81 | 21 | empty |
| 3 | 76 | 0.37 | 0.77 | 15 | empty |
Modifications
Observed in the structure: 15 modified (engineered).
Compared structures
- 4PED · Mitochondrial ADCK3 employs an atypical protein kinase-like fold to enable coenzyme Q… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8NI60 · AlphaFold monomer V2.0 prediction for atypical kinase COQ8A, mitochondrial (Q8NI60) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q8NI60
- Elsewhere: RCSB PDB 4PED · PDBe 4PED · UniProt Q8NI60
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