MolNFT v1 · #69537 · protein
Structure of clpp from bacillus subtilis in monoclinic crystal form
3KTG · ATP-dependent clp protease proteolytic subunit: “Structure of clpp from bacillus subtilis in monoclinic crystal form”. X-ray diffraction, 20 pockets (best druggability 0.63). MolNFT v1 #69537 on GenesisL1: 3D structure, binding…
- PDB
- 3KTG
- Type
- protein
- Length
- 1,316 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 0.63
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 188 | 44% helix, 21% strand | P80244 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 70 | 0.63 | 0.91 | 19 | empty |
| 2 | 64 | 0.63 | 0.92 | 20 | empty |
| 3 | 216 | 0.62 | 0.82 | 20 | empty |
| 4 | 170 | 0.62 | 0.83 | 21 | empty |
| 5 | 213 | 0.61 | 0.81 | 23 | empty |
Interfaces
7 interfaces between chains.
- B–C · 1411 Ų buried · 11 hydrogen bonds · protein-protein
- D–E · 1411 Ų buried · 15 hydrogen bonds · protein-protein
- F–G · 1401 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1395 Ų buried · 11 hydrogen bonds · protein-protein
- E–F · 1385 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 3KTG · Structure of ClpP from Bacillus subtilis in monoclinic 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 0.98
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 3KTG · PDBe 3KTG · UniProt P80244
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