Research workbench
Pandda analysis group deposition -- auto-refined data of AAR2/RNASEH for ground state model 03, dmso-free
Analyse Pandda analysis group deposition -- auto-refined data of AAR2/RNASEH for ground… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5R0P
- Type
- protein
- Length
- 537 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pre-mRNA-splicing factor 8; A1 cistron-splicing factor AAR2
- UniProt
- P33334, P32357
- Pockets
- 6 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 18% 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, 18% strand | P32357 |
Pockets
6 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.40 | 0.75 | 16 | empty |
| 2 | 84 | 0.40 | 0.78 | 19 | empty |
| 3 | 125 | 0.38 | 0.73 | 19 | empty |
| 4 | 108 | 0.37 | 0.74 | 22 | empty |
| 5 | 87 | 0.35 | 0.75 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 473 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 5R0P · PanDDA analysis group deposition -- Auto-refined data of Aar2/RNaseH for ground state… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 5R0P · PDBe 5R0P · UniProt P33334 · UniProt P32357
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