Research workbench
CLPP2 from chlamydia trachomatis with resolved handle loop
Analyse CLPP2 from chlamydia trachomatis with resolved handle loop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6X60
- Type
- protein
- Length
- 1,328 residues
- Chains
- 7
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit 2
- EC
- 3.4.21.92
- UniProt
- Q3KKY8
- Pockets
- 18 · best druggability 0.73
Structure
x-ray diffraction · 6 distinct chains · 42% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 187 | 42% helix, 19% strand | Q3KKY8 |
| B, G | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 192 | 42% helix, 19% strand | Q3KKY8 |
| C | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 189 | 41% helix, 19% strand | Q3KKY8 |
| D | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 187 | 42% helix, 19% strand | Q3KKY8 |
| E | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 193 | 40% helix, 18% strand | Q3KKY8 |
| F | ATP-dependent clp protease proteolytic subunit 2 (EC 3.4.21.92) | protein | 188 | 43% helix, 19% strand | Q3KKY8 |
Pockets
18 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.73 | 0.81 | 90 | empty |
| 2 | 119 | 0.67 | 0.89 | 23 | empty |
| 3 | 412 | 0.67 | 0.80 | 63 | empty |
| 4 | 290 | 0.63 | 0.80 | 49 | empty |
| 5 | 70 | 0.47 | 0.83 | 13 | empty |
Interfaces
7 interfaces between chains.
- D–G · 1573 Ų buried · 15 hydrogen bonds · protein-protein
- B–G · 1537 Ų buried · 12 hydrogen bonds · protein-protein
- A–F · 1510 Ų buried · 13 hydrogen bonds · protein-protein
- C–E · 1493 Ų buried · 11 hydrogen bonds · protein-protein
- B–E · 1491 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 6X60 · ClpP2 from Chlamydia trachomatis with resolved handle loop · the same entry in another collection · chain G against G, TM-score 1.00
- Q3KKY8 · AlphaFold monomer V2.0 prediction for ATP-dependent clp protease proteolytic subunit 2… · a predicted model of the same protein · chain C against A, TM-score 0.91
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 Q3KKY8
- Elsewhere: RCSB PDB 6X60 · PDBe 6X60 · UniProt Q3KKY8
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