Research workbench
Crystal structure of E.COLI lon proteolytic domain
Analyse Crystal 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
- 1RRE
- Type
- protein
- Length
- 1,101 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease la
- EC
- 3.4.21.53
- UniProt
- P0A9M0
- Ligands
- SO4
- Pockets
- 15 · best druggability 0.56
Structure
x-ray diffraction · 3 distinct chains · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ATP-dependent protease la (EC 3.4.21.53) | protein | 182 | 36% helix, 31% strand | P0A9M0 |
| E | ATP-dependent protease la (EC 3.4.21.53) | protein | 191 | 36% helix, 26% strand | P0A9M0 |
| F | ATP-dependent protease la (EC 3.4.21.53) | protein | 182 | 36% helix, 29% strand | P0A9M0 |
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
15 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 161 | 0.56 | 0.81 | 23 | empty |
| 2 | 59 | 0.54 | 0.88 | 15 | empty |
| 3 | 134 | 0.51 | 0.80 | 24 | empty |
| 4 | 140 | 0.49 | 0.79 | 22 | empty |
| 5 | 122 | 0.48 | 0.79 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–F · 789 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 784 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 774 Ų buried · 10 hydrogen bonds · protein-protein
- E–F · 772 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 744 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 19 modified, 6 disulfide (engineered, disulfide).
Compared structures
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 P0A9M0
- Elsewhere: RCSB PDB 1RRE · PDBe 1RRE · UniProt P0A9M0
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