Research workbench
Cryo-EM structure of RAC in the State C2 RNC-RAC complex
Analyse Cryo-EM structure of RAC in the State C2 RNC-RAC complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7X3K
- Type
- protein
- Length
- 768 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 6.0
- Source
- Saccharomyces cerevisiae
- Molecule
- Zuotin; Ribosome-associated complex subunit SSZ1
- UniProt
- P32527, P38788
- Pockets
- 11 · best druggability 0.78
Structure
electron microscopy · resolution 6.0 · 2 distinct chains · 38% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zuotin | protein | 262 | 47% helix, 2% strand | P32527 |
| B | Ribosome-associated complex subunit SSZ1 | protein | 506 | 33% helix, 36% strand | P38788 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.78 | 0.85 | 64 | empty |
| 2 | 743 | 0.73 | 0.79 | 78 | empty |
| 3 | 62 | 0.66 | 0.94 | 16 | empty |
| 4 | 459 | 0.64 | 0.77 | 54 | empty |
| 5 | 138 | 0.57 | 0.83 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 2773 Ų buried · 24 hydrogen bonds · protein-protein
Compared structures
- 7X3K · Cryo-EM structure of rac in the state C2 rnc-rac complex · the same entry in another collection · chain A against A, TM-score 1.00
- P38788 · AlphaFold monomer V2.0 prediction for ribosome-associated complex subunit SSZ1 (P38788) · a predicted model of the same protein · chain B against A, TM-score 0.97
- P32527 · AlphaFold monomer V2.0 prediction for zuotin (P32527) · a predicted model of the same protein · chain A against A, TM-score 0.81
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 P32527
- Every structure of UniProt P38788
- Elsewhere: RCSB PDB 7X3K · PDBe 7X3K · UniProt P32527 · UniProt P38788
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