Research workbench
AlphaFold monomer V2.0 prediction for carboxylesterase 1 (Q0ZPV7)
Analyse AlphaFold monomer V2.0 prediction for carboxylesterase 1 (Q0ZPV7) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q0ZPV7
- Type
- protein
- Length
- 335 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x13D0a95FDcd918ebb5150FD2C57cfC72eC29DA05
- UniProt
- Q0ZPV7
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 335 | — | Q0ZPV7 |
Compared structures
- 2O7R · Plant carboxylesterase AeCXE1 from Actinidia eriantha with acyl adduct · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 2O7R · Plant carboxylesterase AECXE1 from actinidia eriantha with acyl adduct · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 2O7V · Carboxylesterase AeCXE1 from Actinidia eriantha covalently inhibited by paraoxon · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 2O7V · Carboxylesterase AECXE1 from actinidia eriantha covalently inhibited by paraoxon · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 Q0ZPV7
- Elsewhere: UniProt Q0ZPV7 · AlphaFold DB Q0ZPV7
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