Research workbench
AlphaFold monomer V2.0 prediction for formamidopyrimidine-DNA glycosylase (P05523)
Analyse AlphaFold monomer V2.0 prediction for formamidopyrimidine-DNA glycosylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P05523
- Type
- protein
- Length
- 269 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0Bd770503E1bC139C5289bf2beF9d371036A5123
- UniProt
- P05523
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 269 | — | P05523 |
Compared structures
- 1K82 · Crystal structure of E.COLI formamidopyrimidine-DNA glycosylase (fpg) covalently trapped… · an experimental structure of the same protein · chain A against D, TM-score 0.93
- 1K82 · Crystal structure of E.coli formamidopyrimidine-DNA glycosylase (Fpg) covalently trapped… · an experimental structure of the same protein · chain A against D, TM-score 0.93
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 P05523
- Elsewhere: UniProt P05523 · AlphaFold DB P05523
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