Research workbench
Oxidized-form structure of E.COLI lon proteolytic domain
Analyse Oxidized-form structure of E.COLI lon proteolytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WU4
- Type
- protein
- Length
- 1,094 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lon protease
- EC
- 3.4.21.53
- UniProt
- C9QQ79
- Ligands
- SO4
- Pockets
- 12 · best druggability 0.56
Structure
x-ray diffraction · 6 distinct chains · 37% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lon protease (EC 3.4.21.53) | protein | 178 | 36% helix, 31% strand | C9QQ79 |
| B | Lon protease (EC 3.4.21.53) | protein | 180 | 36% helix, 28% strand | C9QQ79 |
| C | Lon protease (EC 3.4.21.53) | protein | 181 | 37% helix, 31% strand | C9QQ79 |
| D | Lon protease (EC 3.4.21.53) | protein | 182 | 36% helix, 30% strand | C9QQ79 |
| E | Lon protease (EC 3.4.21.53) | protein | 194 | 38% helix, 28% strand | C9QQ79 |
| F | Lon protease (EC 3.4.21.53) | protein | 179 | 40% helix, 28% strand | C9QQ79 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.56 | 0.80 | 23 | empty |
| 2 | 217 | 0.56 | 0.79 | 32 | empty |
| 3 | 266 | 0.54 | 0.76 | 29 | empty |
| 4 | 149 | 0.52 | 0.80 | 25 | empty |
| 5 | 150 | 0.50 | 0.78 | 27 | empty |
Interfaces
6 interfaces between chains.
- E–F · 796 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 794 Ų buried · 10 hydrogen bonds · protein-protein
- A–F · 762 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 741 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 738 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3WU4 · Oxidized-form structure of E.coli Lon Proteolytic domain · 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 C9QQ79
- Elsewhere: RCSB PDB 3WU4 · PDBe 3WU4 · UniProt C9QQ79
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