Research workbench
Crystal Structure of E-R ClpX Hexamer
Analyse Crystal Structure of E-R ClpX Hexamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I63
- Type
- protein
- Length
- 1,846 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 5.709
- Source
- Escherichia coli
- Molecule
- ATP-dependent Clp protease ATP-binding subunit ClpX
- UniProt
- P0A6H1
- Ligands
- SO4
- Pockets
- 19 · best druggability 0.83
Structure
x-ray diffraction · resolution 5.709 · 6 distinct chains · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 311 | 52% helix, 11% strand | P0A6H1 |
| B | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 307 | 53% helix, 11% strand | P0A6H1 |
| C | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 298 | 50% helix, 12% strand | P0A6H1 |
| D | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 310 | 53% helix, 11% strand | P0A6H1 |
| E | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 315 | 52% helix, 11% strand | P0A6H1 |
| F | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 305 | 49% helix, 11% strand | P0A6H1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 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
19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 896 | 0.83 | 0.85 | 78 | SO4 |
| 2 | 843 | 0.82 | 0.85 | 77 | SO4 |
| 3 | 1166 | 0.82 | 0.83 | 123 | SO4 |
| 4 | 749 | 0.81 | 0.84 | 82 | SO4 |
| 5 | 739 | 0.77 | 0.81 | 73 | SO4 |
Interfaces
6 interfaces between chains.
- A–B · 1350 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1328 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 1124 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 1105 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 1075 Ų buried · 9 hydrogen bonds · protein-protein
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 P0A6H1
- Elsewhere: RCSB PDB 4I63 · PDBe 4I63 · UniProt P0A6H1
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