Research workbench
AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (P0A6X3)
Analyse AlphaFold monomer V2.0 prediction for RNA-binding protein hfq (P0A6X3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A6X3
- Type
- protein
- Length
- 102 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB35df660264f41795De49C83276C108A4ba91ADE
- UniProt
- P0A6X3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 102 | — | P0A6X3 |
Compared structures
- 4V2S · Crystal structure of hfq in complex with the srna rydc · an experimental structure of the same protein · chain A against F, TM-score 0.65
- 4V2S · Crystal structure of Hfq in complex with the sRNA RydC · an experimental structure of the same protein · chain A against F, TM-score 0.65
- 3QHS · Crystal structure of full-length Hfq from Escherichia coli · an experimental structure of the same protein · chain A against D, TM-score 0.65
- 3QHS · Crystal structure of full-length hfq from escherichia COLI · an experimental structure of the same protein · chain A against D, TM-score 0.65
- 4RCB · Crystal structure of E COLI hfq · an experimental structure of the same protein · chain A against A, TM-score 0.64
- 4RCB · Crystal structure of E Coli Hfq · an experimental structure of the same protein · chain A against A, TM-score 0.64
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 P0A6X3
- Elsewhere: UniProt P0A6X3 · AlphaFold DB P0A6X3
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