Research workbench
Single-particle cryo-EM of co-translational folded adr1 domain inside the E. coli ribosome exit tunnel.
Analyse Single-particle cryo-EM of co-translational folded adr1 domain inside the E.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A7U
- Type
- protein
- Length
- 27 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 4.8
- Source
- SACCHAROMYCES CEREVISIAE
- Molecule
- Regulatory protein ADR1
- UniProt
- P07248
- Ligands
- ZN
Structure
electron microscopy · resolution 4.8 · 1 distinct chain · 30% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulatory protein ADR1 | protein | 27 | 30% helix, 7% strand | P07248 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5A7U · Single-particle cryo-EM of co-translational folded ADR1 domain inside the E. COLI… · the same entry in another collection · chain A against A, TM-score 1.00
- P07248 · AlphaFold monomer V2.0 prediction for regulatory protein ADR1 (P07248) · a predicted model of the same protein · chain A against A, TM-score 0.57
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 P07248
- Elsewhere: RCSB PDB 5A7U · PDBe 5A7U · UniProt P07248
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