Research workbench
Caseinolytic protease (clpp) from staphylococcus aureus mutant - V7A
Analyse Caseinolytic protease (clpp) from staphylococcus aureus mutant - V7A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DKF
- Type
- protein
- Length
- 2,314 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- A6QF76
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 3 distinct chains · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, D, C, E, F, I, K, J, L, M | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 165 | 48% helix, 18% strand | A6QF76 |
| A, H | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 168 | 47% helix, 18% strand | A6QF76 |
| G, N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 164 | 48% helix, 18% strand | A6QF76 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 801 | 0.78 | 0.82 | 108 | empty |
| 2 | 935 | 0.77 | 0.80 | 115 | empty |
| 3 | 270 | 0.66 | 0.82 | 51 | empty |
| 4 | 312 | 0.65 | 0.81 | 50 | empty |
| 5 | 72 | 0.55 | 0.87 | 20 | empty |
Interfaces
27 interfaces between chains.
- F–G · 1182 Ų buried · 10 hydrogen bonds · protein-protein
- I–J · 1178 Ų buried · 7 hydrogen bonds · protein-protein
- M–N · 1167 Ų buried · 10 hydrogen bonds · protein-protein
- K–L · 1163 Ų buried · 8 hydrogen bonds · protein-protein
- D–E · 1163 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6DKF · Caseinolytic protease (ClpP) from Staphylococcus aureus mutant - V7A · the same entry in another collection · chain H against H, 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 A6QF76
- Elsewhere: RCSB PDB 6DKF · PDBe 6DKF · UniProt A6QF76
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.