Research workbench
S.AUREUS clpc resting state, C2 symmetrised
Analyse S.AUREUS clpc resting state, C2 symmetrised in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EM8
- Type
- protein
- Length
- 6,378 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease ATP-binding subunit clpc
- UniProt
- W8U1E4
- Pockets
- 20 · best druggability 0.68
Structure
electron microscopy · 5 distinct chains · 41% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, F, G | ATP-dependent clp protease ATP-binding subunit clpc | protein | 744 | 43% helix, 4% strand | W8U1E4 |
| C, H | ATP-dependent clp protease ATP-binding subunit clpc | protein | 602 | 45% helix, 8% strand | W8U1E4 |
| D, I | ATP-dependent clp protease ATP-binding subunit clpc | protein | 436 | 43% helix, 3% strand | W8U1E4 |
| E | ATP-dependent clp protease ATP-binding subunit clpc | protein | 664 | 38% helix, 5% strand | W8U1E4 |
| L | ATP-dependent clp protease ATP-binding subunit clpc | protein | 662 | 40% helix, 8% strand | W8U1E4 |
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 | 711 | 0.68 | 0.77 | 102 | empty |
| 2 | 827 | 0.68 | 0.75 | 123 | empty |
| 3 | 954 | 0.67 | 0.74 | 114 | empty |
| 4 | 1188 | 0.67 | 0.74 | 156 | empty |
| 5 | 644 | 0.66 | 0.77 | 90 | empty |
Interfaces
17 interfaces between chains.
- E–F · 1373 Ų buried · 35 hydrogen bonds · protein-protein
- C–D · 719 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 603 Ų buried · 20 hydrogen bonds · protein-protein
- F–G · 578 Ų buried · 21 hydrogen bonds · protein-protein
- A–L · 573 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 6EM8 · S.aureus ClpC resting state, C2 symmetrised · 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 W8U1E4
- Elsewhere: RCSB PDB 6EM8 · PDBe 6EM8 · UniProt W8U1E4
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