Research workbench
Crystal structure of Q9PR55 at pH 6.0 (use NMR model)
Analyse Crystal structure of Q9PR55 at pH 6.0 (use NMR model) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8W68
- Type
- protein
- Length
- 627 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Ureaplasma parvum serovar 3 str. ATCC 700970
- Molecule
- Uncharacterized protein UU089.1
- UniProt
- Q9PR55
- Pockets
- 11 · best druggability 0.55
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 9% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, H | Uncharacterized protein UU089.1 | protein | 79 | 9% helix, 43% strand | Q9PR55 |
| B, C, E, F, G | Uncharacterized protein UU089.1 | protein | 78 | 9% helix, 42% strand | Q9PR55 |
Pockets
11 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.55 | 0.75 | 44 | empty |
| 2 | 148 | 0.44 | 0.75 | 21 | empty |
| 3 | 55 | 0.43 | 0.82 | 11 | empty |
| 4 | 56 | 0.42 | 0.82 | 10 | empty |
| 5 | 59 | 0.41 | 0.81 | 11 | empty |
Interfaces
9 interfaces between chains.
- A–B · 525 Ų buried · 3 hydrogen bonds · protein-protein
- D–F · 512 Ų buried · 3 hydrogen bonds · protein-protein
- C–E · 504 Ų buried · 1 hydrogen bond · protein-protein
- G–H · 502 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 494 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- Q9PR55 · AlphaFold monomer V2.0 prediction for uncharacterized protein UU089.1 (Q9PR55) · 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 Q9PR55
- Elsewhere: RCSB PDB 8W68 · PDBe 8W68 · UniProt Q9PR55
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