Research workbench
AlphaFold monomer V2.0 prediction for cyclic ump-AMP synthase (G2SLH8)
Analyse AlphaFold monomer V2.0 prediction for cyclic ump-AMP synthase (G2SLH8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G2SLH8
- Type
- protein
- Length
- 288 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- UniProt
- G2SLH8
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 288 | — | G2SLH8 |
Compared structures
- 6E0L · Structure of rhodothermus marinus cdne C-ump-AMP synthase with apcpp and upnpp · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 6E0L · Structure of Rhodothermus marinus CdnE c-UMP-AMP synthase with Apcpp and Upnpp · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 6E0K · Structure of rhodothermus marinus cdne C-ump-AMP synthase · an experimental structure of the same protein · chain A against A, TM-score 0.96
- 6E0K · Structure of Rhodothermus marinus CdnE c-UMP-AMP synthase · an experimental structure of the same protein · chain A against A, TM-score 0.96
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 G2SLH8
- Elsewhere: UniProt G2SLH8 · AlphaFold DB G2SLH8
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