Research workbench
Structure of clpp from bacillus subtilis in orthorombic crystal form
Analyse Structure of clpp from bacillus subtilis in orthorombic crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KTH
- Type
- protein
- Length
- 1,267 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- P80244
- Pockets
- 20 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 47% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 180 | 47% helix, 22% strand | P80244 |
| B, F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 182 | 47% helix, 21% strand | P80244 |
| D, E, G | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 181 | 47% helix, 20% strand | P80244 |
Pockets
20 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.64 | 0.93 | 18 | empty |
| 2 | 53 | 0.62 | 0.93 | 19 | empty |
| 3 | 50 | 0.59 | 0.92 | 19 | empty |
| 4 | 150 | 0.47 | 0.76 | 25 | empty |
| 5 | 188 | 0.47 | 0.75 | 22 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1528 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 1457 Ų buried · 12 hydrogen bonds · protein-protein
- A–G · 1452 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1447 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 1430 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3KTH · Structure of ClpP from Bacillus subtilis in orthorombic crystal form · the same entry in another collection · chain G against G, TM-score 1.00
- P80244 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P80244
- Elsewhere: RCSB PDB 3KTH · PDBe 3KTH · UniProt P80244
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