Research workbench
Crystal structure of an Aar2p S253E phosphomimetic mutant protein
Analyse Crystal structure of an Aar2p S253E phosphomimetic mutant protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ILI
- Type
- protein
- Length
- 582 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.2046
- Source
- Saccharomyces cerevisiae
- Molecule
- A1 cistron-splicing factor AAR2
- UniProt
- P32357
- Pockets
- 6 · best druggability 0.81
Structure
x-ray diffraction · resolution 3.2046 · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | A1 cistron-splicing factor AAR2 | protein | 290 | 37% helix, 17% strand | P32357 |
| B | A1 cistron-splicing factor AAR2 | protein | 292 | 35% helix, 18% strand | P32357 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 964 | 0.81 | 0.83 | 101 | empty |
| 2 | 135 | 0.70 | 0.90 | 25 | empty |
| 3 | 64 | 0.70 | 0.95 | 20 | empty |
| 4 | 91 | 0.41 | 0.78 | 20 | empty |
| 5 | 59 | 0.34 | 0.77 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 574 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4ILI · Crystal structure of an AAR2P S253E phosphomimetic mutant protein · 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 A against A, TM-score 0.93
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
- Elsewhere: RCSB PDB 4ILI · PDBe 4ILI · UniProt P32357
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