MolNFT v1 · #389305 · protein
AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit omega (A1AHI0)
A1AHI0: “AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit omega (A1AHI0)”. MolNFT v1 #389305 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- A1AHI0
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- DNA-directed RNA polymerase subunit omega
- UniProt
- A1AHI0
Structure
1 distinct chain · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA-directed RNA polymerase subunit omega | protein | 91 | 67% helix, 0% strand | A1AHI0 |
Compared structures
- 9DR1 · E. coli RNA polymerase consensus volume with a bound fluoride riboswitch in the… · an experimental structure of the same protein · chain A against K, TM-score 0.83
- 8F3C · Cryo-EM consensus structure of Escherichia coli que-PEC (paused elongation complex) RNA… · an experimental structure of the same protein · chain A against K, TM-score 0.83
- 8G4W · Cryo-EM consensus structure of Escherichia coli que-PEC (paused elongation complex) RNA… · an experimental structure of the same protein · chain A against K, TM-score 0.82
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 A1AHI0
- Elsewhere: UniProt A1AHI0 · AlphaFold DB A1AHI0
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