MolNFT v1 · #183158 · protein
R-state of wild type human mitochondrial LONP1 protease bound to endogenous ADP
7NGL · Lon protease homolog, mitochondrial: “R-state of wild type human mitochondrial LONP1 protease bound to endogenous ADP”. Electron microscopy, 1 ligand (ADP), 20 pockets (best druggability 0.83). MolNFT v1 #183158 on GenesisL1: 3D…
- PDB
- 7NGL
- Type
- protein
- Length
- 4,656 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lon protease homolog, mitochondrial
- EC
- 3.4.21.53
- UniProt
- P36776
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 45% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Lon protease homolog, mitochondrial (EC 3.4.21.53) | protein | 776 | 45% helix, 10% strand | P36776 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 748 | 0.83 | 0.86 | 92 | empty |
| 2 | 918 | 0.82 | 0.83 | 98 | empty |
| 3 | 903 | 0.79 | 0.81 | 89 | empty |
| 4 | 728 | 0.79 | 0.83 | 73 | empty |
| 5 | 950 | 0.79 | 0.81 | 82 | ADP |
Interfaces
15 interfaces between chains.
- C–D · 2567 Ų buried · 25 hydrogen bonds · protein-protein
- A–B · 2509 Ų buried · 22 hydrogen bonds · protein-protein
- E–F · 2470 Ų buried · 22 hydrogen bonds · protein-protein
- A–F · 2251 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 2161 Ų buried · 25 hydrogen bonds · protein-protein
Compared structures
- 7NGL · R-state of wild type human mitochondrial LONP1 protease bound to endogenous ADP · the same entry in another collection · chain A against A, TM-score 1.00
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 P36776
- Elsewhere: RCSB PDB 7NGL · PDBe 7NGL · UniProt P36776
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