Research workbench
Crystal Structure of W-W-W ClpX Hexamer
Analyse Crystal Structure of W-W-W ClpX Hexamer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I34
- Type
- protein
- Length
- 1,833 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.1218
- Source
- Escherichia coli
- Molecule
- ATP-dependent Clp protease ATP-binding subunit ClpX
- UniProt
- P0A6H1
- Ligands
- SO4
- Pockets
- 14 · best druggability 0.85
Structure
x-ray diffraction · resolution 4.1218 · 6 distinct chains · 49% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 316 | 49% helix, 12% strand | P0A6H1 |
| B | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 312 | 48% helix, 12% strand | P0A6H1 |
| C | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 303 | 48% helix, 13% strand | P0A6H1 |
| D | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 295 | 49% helix, 13% strand | P0A6H1 |
| E | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 301 | 48% helix, 13% strand | P0A6H1 |
| F | ATP-dependent Clp protease ATP-binding subunit ClpX | protein | 306 | 49% helix, 13% 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
14 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1005 | 0.85 | 0.86 | 87 | SO4 |
| 2 | 963 | 0.85 | 0.86 | 90 | SO4 |
| 3 | 1089 | 0.83 | 0.84 | 84 | SO4 |
| 4 | 978 | 0.83 | 0.84 | 85 | SO4 |
| 5 | 1049 | 0.79 | 0.80 | 111 | SO4 |
Interfaces
6 interfaces between chains.
- E–F · 1565 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 1531 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1451 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1429 Ų buried · 8 hydrogen bonds · protein-protein
- A–F · 1071 Ų buried · 7 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 4I34 · PDBe 4I34 · UniProt P0A6H1
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