Research workbench
Crystal structure of H.pylori ClpP
Analyse Crystal structure of H.pylori ClpP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZL0
- Type
- protein
- Length
- 2,422 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.6
- Source
- Helicobacter pylori
- Molecule
- ATP-dependent Clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- P56156
- Pockets
- 20 · best druggability 0.70
Structure
x-ray diffraction · resolution 2.6 · 1 distinct chain · 45% 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 | 173 | 45% helix, 26% strand | P56156 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 671 | 0.70 | 0.77 | 92 | empty |
| 2 | 481 | 0.67 | 0.78 | 76 | empty |
| 3 | 561 | 0.65 | 0.76 | 74 | empty |
| 4 | 566 | 0.65 | 0.76 | 74 | empty |
| 5 | 580 | 0.64 | 0.75 | 62 | empty |
Interfaces
35 interfaces between chains.
- A–B · 1192 Ų buried · 10 hydrogen bonds · protein-protein
- M–N · 1172 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1171 Ų buried · 13 hydrogen bonds · protein-protein
- J–K · 1166 Ų buried · 14 hydrogen bonds · protein-protein
- A–G · 1160 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2ZL0 · Crystal structure of H.PYLORI clpp · the same entry in another collection · chain K against K, 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 P56156
- Elsewhere: RCSB PDB 2ZL0 · PDBe 2ZL0 · UniProt P56156
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