Research workbench
AlphaFold monomer V2.0 prediction for 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (O43598)
Analyse AlphaFold monomer V2.0 prediction for 2'-deoxynucleoside 5'-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O43598
- Type
- protein
- Length
- 174 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x805108b3adf62349cD15C1e3fD96fa37c0792E36
- UniProt
- O43598
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 174 | — | O43598 |
Compared structures
- 8QHQ · Crystal structure of human DNPH1 bound to hmdUMP · an experimental structure of the same protein · chain A against C, TM-score 0.80
- 4P5E · Crystal structure of human DNPH1 (rcl) with 6-naphthyl-purine-riboside-monophosphate · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 4P5E · Crystal structure of human DNPH1 (rcl) with 6-naphthyl-purine- riboside-monophosphate · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 8QHR · Crystal structure of the human DNPH1 glycosyl-enzyme intermediate · an experimental structure of the same protein · chain A against A, TM-score 0.74
- 8RPT · Crystal structure of human DNPH1 mutant- D80A · an experimental structure of the same protein · chain A against B, TM-score 0.73
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 O43598
- Elsewhere: UniProt O43598 · AlphaFold DB O43598
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