Research workbench
PanDDA analysis group deposition -- Aar2/RNaseH in complex with fragment P04G11 from the F2X-Universal Library
Analyse PanDDA analysis group deposition -- Aar2/RNaseH in complex with fragment P04G11… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FL0
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.51
- Source
- Saccharomyces cerevisiae S288C
- Molecule
- Pre-mRNA-splicing factor 8; A1 cistron-splicing factor AAR2
- UniProt
- P33334, P32357
- Ligands
- VNX
- Pockets
- 8 · best druggability 0.48
Structure
x-ray diffraction · resolution 1.51 · 2 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pre-mRNA-splicing factor 8 | protein | 237 | 46% helix, 19% strand | P33334 |
| B | A1 cistron-splicing factor AAR2 | protein | 300 | 45% helix, 19% strand | P32357 |
Ligands and binding sites
- VNX · 5-cyclopropyl-2H-tetrazole · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.48 | 0.84 | 12 | empty |
| 2 | 90 | 0.41 | 0.78 | 18 | empty |
| 3 | 116 | 0.41 | 0.76 | 16 | empty |
| 4 | 73 | 0.37 | 0.77 | 16 | empty |
| 5 | 96 | 0.34 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 485 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- P32357 · AlphaFold monomer V2.0 prediction for A1 cistron-splicing factor AAR2 (P32357) · a predicted model of the same protein · chain B 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 P33334
- Every structure of UniProt P32357
- Elsewhere: RCSB PDB 7FL0 · PDBe 7FL0 · UniProt P33334 · UniProt P32357
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