Research workbench
Compressed conformation of francisella tularensis clpp at 2.84 a
Analyse Compressed conformation of francisella tularensis clpp at 2.84 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5G1Q
- Type
- protein
- Length
- 1,217 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clp protease proteolytic subunit P
- EC
- 3.4.21.92
- UniProt
- Q5NH47
- Pockets
- 20 · best druggability 0.75
Structure
x-ray diffraction · 7 distinct chains · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 181 | 39% helix, 23% strand | Q5NH47 |
| B | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 172 | 42% helix, 23% strand | Q5NH47 |
| C | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 175 | 41% helix, 21% strand | Q5NH47 |
| D | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 170 | 44% helix, 19% strand | Q5NH47 |
| E | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 171 | 43% helix, 20% strand | Q5NH47 |
| F | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 171 | 42% helix, 23% strand | Q5NH47 |
| G | Clp protease proteolytic subunit P (EC 3.4.21.92) | protein | 177 | 40% helix, 22% strand | Q5NH47 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1131 | 0.75 | 0.78 | 99 | empty |
| 2 | 126 | 0.67 | 0.89 | 28 | empty |
| 3 | 188 | 0.61 | 0.82 | 19 | empty |
| 4 | 150 | 0.58 | 0.83 | 22 | empty |
| 5 | 211 | 0.56 | 0.78 | 23 | empty |
Interfaces
9 interfaces between chains.
- A–G · 1653 Ų buried · 24 hydrogen bonds · protein-protein
- B–C · 1586 Ų buried · 14 hydrogen bonds · protein-protein
- F–G · 1540 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1491 Ų buried · 19 hydrogen bonds · protein-protein
- E–F · 1463 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 5G1Q · Compressed conformation of Francisella tularensis ClpP at 2.84 A · the same entry in another collection · chain G against G, TM-score 1.00
- Q5NH47 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic subunit… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q5NH47
- Elsewhere: RCSB PDB 5G1Q · PDBe 5G1Q · UniProt Q5NH47
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