Research workbench
AlphaFold monomer V2.0 prediction for ectonucleoside triphosphate diphosphohydrolase 1 (P97687)
Analyse AlphaFold monomer V2.0 prediction for ectonucleoside triphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P97687
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3C8340d0a867aE99943D11461e905F0d1C49C9ad
- UniProt
- P97687
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 511 | — | P97687 |
Compared structures
- 3ZX3 · Crystal structure and domain rotation of NTPDASE1 CD39 · an experimental structure of the same protein · chain A against A, TM-score 0.76
- 3ZX3 · Crystal Structure and Domain Rotation of NTPDase1 CD39 · an experimental structure of the same protein · chain A against A, TM-score 0.76
- 3ZX2 · NTPDASE1 in complex with decavanadate · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 3ZX2 · NTPDase1 in complex with Decavanadate · an experimental structure of the same protein · chain A against B, TM-score 0.76
- 3ZX0 · NTPDase1 in complex with Heptamolybdate · an experimental structure of the same protein · chain A against D, TM-score 0.75
- 3ZX0 · NTPDASE1 in complex with heptamolybdate · an experimental structure of the same protein · chain A against D, 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 P97687
- Elsewhere: UniProt P97687 · AlphaFold DB P97687
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