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Crystal structure of the ATP-dependent clp protease proteolytic subunit 1 (CLPP1) from mycobacterium tuberculosis
Analyse Crystal structure of the ATP-dependent clp protease proteolytic subunit 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CE3
- Type
- protein
- Length
- 2,342 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit 1
- EC
- 3.4.21.92
- UniProt
- P0A526
- Pockets
- 20 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 51% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F, G, H, I, J, K, M, N | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 167 | 51% helix, 20% strand | P0A526 |
| E, L | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 169 | 50% helix, 20% strand | P0A526 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 174 | 0.61 | 0.83 | 25 | empty |
| 2 | 169 | 0.59 | 0.82 | 20 | empty |
| 3 | 195 | 0.59 | 0.81 | 22 | empty |
| 4 | 192 | 0.59 | 0.81 | 24 | empty |
| 5 | 167 | 0.57 | 0.81 | 21 | empty |
Interfaces
22 interfaces between chains.
- K–L · 1411 Ų buried · 13 hydrogen bonds · protein-protein
- D–E · 1400 Ų buried · 16 hydrogen bonds · protein-protein
- A–G · 1349 Ų buried · 16 hydrogen bonds · protein-protein
- E–F · 1347 Ų buried · 15 hydrogen bonds · protein-protein
- M–N · 1341 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2CE3 · Crystal structure of the ATP-dependent clp protease proteolytic subunit 1 (CLPP1) from… · the same entry in another collection · chain F against F, TM-score 1.00
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 P0A526
- Elsewhere: RCSB PDB 2CE3 · PDBe 2CE3 · UniProt P0A526
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