MolNFT v1 · #183163 · protein
Human mitochondrial lon protease homolog, D2-state
7NGQ · Lon protease homolog, mitochondrial: “Human mitochondrial lon protease homolog, D2-state”. Electron microscopy, 1 ligand (ADP), 20 pockets (best druggability 0.86). MolNFT v1 #183163 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7NGQ
- 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 0.86
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 | 992 | 0.86 | 0.87 | 124 | empty |
| 2 | 1159 | 0.85 | 0.86 | 121 | empty |
| 3 | 1131 | 0.82 | 0.83 | 108 | empty |
| 4 | 1038 | 0.81 | 0.82 | 80 | empty |
| 5 | 780 | 0.80 | 0.84 | 95 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1769 Ų buried · 19 hydrogen bonds · protein-protein
- A–F · 1759 Ų buried · 31 hydrogen bonds · protein-protein
- C–D · 1746 Ų buried · 39 hydrogen bonds · protein-protein
- D–E · 1634 Ų buried · 73 hydrogen bonds · protein-protein
- E–F · 1478 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 7NGQ · Human mitochondrial Lon protease homolog, D2-state · 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 7NGQ · PDBe 7NGQ · UniProt P36776
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