Research workbench
Gu_alpha_helicase
Analyse Gu_alpha_helicase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZIN
- Type
- protein
- Length
- 445 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- MUS MUSCULUS
- Molecule
- Importin subunit alpha-2; Nucleolar RNA helicase 2
- EC
- 3.6.4.13
- UniProt
- P52293, Q9JIK5
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · resolution 2 · 3 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Importin subunit alpha-2 | protein | 426 | 74% helix, 0% strand | P52293 |
| B | Nucleolar RNA helicase 2 (EC 3.6.4.13) | protein | 13 | 38% helix, 0% strand | Q9JIK5 |
| C | Nucleolar RNA helicase 2 (EC 3.6.4.13) | protein | 6 | 0% helix, 0% strand | Q9JIK5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.43 | 0.81 | 13 | empty |
| 2 | 53 | 0.29 | 0.75 | 11 | empty |
Interfaces
2 interfaces between chains.
- A–B · 730 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 586 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3ZIN · GU_ALPHA_HELICASE · the same entry in another collection · chain A against A, TM-score 1.00
- P52293 · AlphaFold monomer V2.0 prediction for importin subunit alpha-1 (P52293) · a predicted model of the same protein · chain A against A, TM-score 0.99
- Q9JIK5 · AlphaFold monomer V2.0 prediction for nucleolar RNA helicase 2 (Q9JIK5) · a predicted model of the same protein · chain C against A, TM-score 0.75
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 P52293
- Every structure of UniProt Q9JIK5
- Elsewhere: RCSB PDB 3ZIN · PDBe 3ZIN · UniProt P52293 · UniProt Q9JIK5
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