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Crystal structure of PRP8:AAR2 complex
Analyse Crystal structure of PRP8:AAR2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4I43
- Type
- protein
- Length
- 1,741 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- A1 cistron-splicing factor AAR2; Pre-mRNA-splicing factor 8
- UniProt
- P32357, P33334
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A1 cistron-splicing factor AAR2 | protein | 334 | 40% helix, 18% strand | P32357 |
| B | Pre-mRNA-splicing factor 8 | protein | 1407 | 40% helix, 19% strand | P33334 |
Pockets
20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 994 | 0.81 | 0.82 | 121 | empty |
| 2 | 1141 | 0.77 | 0.79 | 107 | empty |
| 3 | 480 | 0.71 | 0.81 | 49 | empty |
| 4 | 880 | 0.71 | 0.76 | 77 | empty |
| 5 | 643 | 0.69 | 0.77 | 75 | empty |
Interfaces
1 interface between chains.
- A–B · 3705 Ų buried · 48 hydrogen bonds · protein-protein
Compared structures
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 P32357
- Every structure of UniProt P33334
- Elsewhere: RCSB PDB 4I43 · PDBe 4I43 · UniProt P32357 · UniProt P33334
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