Research workbench
Structure of clpp from bacillus subtilis in compressed state
Analyse Structure of clpp from bacillus subtilis in compressed state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TT6
- Type
- protein
- Length
- 1,128 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
- 17 · best druggability 0.46
Structure
x-ray diffraction · 5 distinct chains · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 162 | 48% helix, 20% strand | P80244 |
| C | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 161 | 48% helix, 20% strand | P80244 |
| E | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 160 | 48% helix, 21% strand | P80244 |
| F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 160 | 49% helix, 21% strand | P80244 |
| G | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 161 | 48% helix, 20% strand | P80244 |
Pockets
17 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.46 | 0.79 | 22 | empty |
| 2 | 90 | 0.43 | 0.79 | 19 | empty |
| 3 | 102 | 0.43 | 0.78 | 26 | empty |
| 4 | 96 | 0.42 | 0.78 | 24 | empty |
| 5 | 113 | 0.38 | 0.73 | 19 | empty |
Interfaces
7 interfaces between chains.
- F–G · 952 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 930 Ų buried · 6 hydrogen bonds · protein-protein
- E–F · 922 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 918 Ų buried · 7 hydrogen bonds · protein-protein
- A–G · 907 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3TT6 · Structure of ClpP from Bacillus subtilis in compressed state · 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 F against A, TM-score 0.96
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 3TT6 · PDBe 3TT6 · UniProt P80244
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