Research workbench
AlphaFold monomer V2.0 prediction for ctd nuclear envelope phosphatase 1 (O95476)
Analyse AlphaFold monomer V2.0 prediction for ctd nuclear envelope phosphatase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O95476
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE83892548e88C098Ea0eB1D6dAb6CCCF839Ad27B
- UniProt
- O95476
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 244 | — | O95476 |
Compared structures
- 8UJM · Crystal structure of human CTDNEP1-NEP1R1 protein phosphatase complex with magnesium · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 8UJL · Crystal structure of human CTDNEP1-NEP1R1 protein phosphatase complex · an experimental structure of the same protein · chain A against A, TM-score 0.75
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 O95476
- Elsewhere: UniProt O95476 · AlphaFold DB O95476
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