Research workbench
CLPP1P2 complex from M. tuberculosis
Analyse CLPP1P2 complex from M. tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VGK
- Type
- protein
- Length
- 2,513 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit 2; ATP-dependent clp protease proteolytic…
- EC
- 3.4.21.92
- UniProt
- P9WPC3, P9WPC5
- Pockets
- 20 · best druggability 0.71
Structure
electron microscopy · 2 distinct chains · 46% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 181 | 43% helix, 18% strand | P9WPC3 |
| H, I, J, K, L, M, N | ATP-dependent clp protease proteolytic subunit 1 (EC 3.4.21.92) | protein | 178 | 49% helix, 18% strand | P9WPC5 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 679 | 0.71 | 0.78 | 79 | empty |
| 2 | 600 | 0.66 | 0.76 | 56 | empty |
| 3 | 599 | 0.65 | 0.76 | 62 | empty |
| 4 | 569 | 0.65 | 0.76 | 56 | empty |
| 5 | 598 | 0.65 | 0.76 | 60 | empty |
Interfaces
28 interfaces between chains.
- E–F · 1377 Ų buried · 12 hydrogen bonds · protein-protein
- F–G · 1377 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 1376 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 1374 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 1374 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 6VGK · ClpP1P2 complex from M. tuberculosis · the same entry in another collection · chain J against J, 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 P9WPC3
- Every structure of UniProt P9WPC5
- Elsewhere: RCSB PDB 6VGK · PDBe 6VGK · UniProt P9WPC3 · UniProt P9WPC5
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