Research workbench
Prp8 RH domain from C. merolae
Analyse Prp8 RH domain from C. merolae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NQI
- Type
- protein
- Length
- 383 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.75
- Source
- Cyanidioschyzon merolae (strain 10D)
- Molecule
- Pre-mRNA splicing factor PRP8
- UniProt
- M1V7K2
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · resolution 2.75 · 2 distinct chains · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA splicing factor PRP8 | protein | 196 | 46% helix, 20% strand | M1V7K2 |
| B | Pre-mRNA splicing factor PRP8 | protein | 187 | 45% helix, 18% strand | M1V7K2 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.56 | 0.76 | 22 | empty |
| 2 | 136 | 0.37 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 562 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 6NQI · PRP8 rh domain from C. merolae · 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 M1V7K2
- Elsewhere: RCSB PDB 6NQI · PDBe 6NQI · UniProt M1V7K2
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