Research workbench
AlphaFold monomer V2.0 prediction for spbeta prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase yoss (O34919)
Analyse AlphaFold monomer V2.0 prediction for spbeta prophage-derived deoxyuridine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O34919
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7FDF8b382C6a36A8772D1A265E8e480c7DF0A9C1
- Molecule
- Spbeta prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase yoss
- UniProt
- O34919
Structure
1 distinct chain · 4% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spbeta prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase yoss | protein | 142 | 4% helix, 36% strand | O34919 |
Compared structures
- 4AO5 · B. subtilis prophage dutpase yoss in complex with dump · an experimental structure of the same protein · chain A against B, TM-score 0.88
- 4AO5 · B. subtilis prophage dUTPase YosS in complex with dUMP · an experimental structure of the same protein · chain A against B, TM-score 0.88
- 2XY3 · Structure of the bacillus subtilis prophage dutpase with dupnhpp · an experimental structure of the same protein · chain A against D, TM-score 0.87
- 2XY3 · Structure of the Bacillus subtilis prophage dUTPase with dUpNHpp · an experimental structure of the same protein · chain A against D, TM-score 0.87
- 2Y1T · Bacillus subtilis prophage dUTPase in complex with dUDP · an experimental structure of the same protein · chain A against E, TM-score 0.87
- 2Y1T · Bacillus subtilis prophage dutpase in complex with dudp · an experimental structure of the same protein · chain A against E, TM-score 0.87
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 O34919
- Elsewhere: UniProt O34919 · AlphaFold DB O34919
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