Research workbench
Structure of clpp from staphylococcus aureus (apo, closed state)
Analyse Structure of clpp from staphylococcus aureus (apo, closed state) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TTY
- Type
- protein
- Length
- 2,666 residues
- Chains
- 14
- 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
- A0A077UUA2
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 7 distinct chains · 44% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, G, N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 191 | 43% helix, 28% strand | A0A077UUA2 |
| C | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 187 | 44% helix, 24% strand | A0A077UUA2 |
| E, J, K, M | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 190 | 43% helix, 28% strand | A0A077UUA2 |
| F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 191 | 45% helix, 24% strand | A0A077UUA2 |
| H | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 181 | 46% helix, 24% strand | A0A077UUA2 |
| I | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 199 | 42% helix, 28% strand | A0A077UUA2 |
| L | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 193 | 45% helix, 23% strand | A0A077UUA2 |
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 | 915 | 0.75 | 0.79 | 75 | empty |
| 2 | 314 | 0.74 | 0.86 | 53 | empty |
| 3 | 51 | 0.68 | 0.97 | 16 | empty |
| 4 | 63 | 0.65 | 0.93 | 17 | empty |
| 5 | 307 | 0.64 | 0.80 | 40 | empty |
Interfaces
44 interfaces between chains.
- H–I · 1900 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1884 Ų buried · 17 hydrogen bonds · protein-protein
- K–L · 1777 Ų buried · 16 hydrogen bonds · protein-protein
- C–D · 1773 Ų buried · 18 hydrogen bonds · protein-protein
- F–G · 1771 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6TTY · Structure of ClpP from Staphylococcus aureus (apo, closed state) · the same entry in another collection · chain A against A, 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 A0A077UUA2
- Elsewhere: RCSB PDB 6TTY · PDBe 6TTY · UniProt A0A077UUA2
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