MolNFT v1 · #126322 · protein
AlphaFold monomer V2.0 prediction for feruloyl esterase a (O42807)
O42807: “AlphaFold monomer V2.0 prediction for feruloyl esterase a (O42807)”. MolNFT v1 #126322 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O42807
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xA2DE07e86E532FF47B5d470f3bF914a5B7AafF8c
- UniProt
- O42807
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 281 | — | O42807 |
Compared structures
- 2IX9 · Respective role of protein folding and glycosylation in the thermal stability of… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 2IX9 · Respective role of protein folding and glycosylation in the thermal stability of… · an experimental structure of the same protein · chain A against B, TM-score 0.92
- 2HL6 · Structure of homologously expressed Ferrulate esterase of Aspergillus niger in complex… · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 2HL6 · Structure of homologously expressed ferrulate esterase of aspergillus niger in complex… · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 1UWC · Feruloyl esterase from aspergillus niger · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 1UWC · Feruloyl esterase from Aspergillus niger · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 2BJH · Crystal structure of S133A anfaea-ferulic acid complex · an experimental structure of the same protein · chain A against A, TM-score 0.92
- 2BJH · Crystal Structure Of S133A AnFaeA-ferulic acid complex · an experimental structure of the same protein · chain A against A, TM-score 0.92
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 O42807
- Elsewhere: UniProt O42807 · AlphaFold DB O42807
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