Research workbench
Clpp and clpx igf loop in clpx-clpp complex with D7 symmetry
Analyse Clpp and clpx igf loop in clpx-clpp complex with D7 symmetry in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PPE
- Type
- protein
- Length
- 2,814 residues
- Chains
- 28
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit; ATP-dependent clp protease ATP-binding…
- EC
- 3.4.21.92
- UniProt
- A0A0K4NM46, A0A1Q9L861
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 2 distinct chains · 42% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 192 | 44% helix, 28% strand | A0A0K4NM46 |
| O, P, Q, R, S, T, U, V, X, Y, Z, 1, 2, 3 | ATP-dependent clp protease ATP-binding subunit clpx | protein | 9 | 0% helix, 0% strand | A0A1Q9L861 |
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 689 | 0.78 | 0.83 | 97 | empty |
| 2 | 930 | 0.78 | 0.80 | 115 | empty |
| 3 | 620 | 0.77 | 0.82 | 84 | empty |
| 4 | 705 | 0.75 | 0.80 | 86 | empty |
| 5 | 723 | 0.75 | 0.80 | 85 | empty |
Interfaces
63 interfaces between chains.
- H–N · 1749 Ų buried · 20 hydrogen bonds · protein-protein
- M–N · 1744 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 1742 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1742 Ų buried · 18 hydrogen bonds · protein-protein
- J–K · 1742 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6PPE · ClpP and ClpX IGF loop in ClpX-ClpP complex with D7 symmetry · the same entry in another collection · chain B against B, 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 A0A0K4NM46
- Every structure of UniProt A0A1Q9L861
- Elsewhere: RCSB PDB 6PPE · PDBe 6PPE · UniProt A0A0K4NM46 · UniProt A0A1Q9L861
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