Research workbench
AlphaFold monomer V2.0 prediction for bifunctional XYLANASE/DEACETYLASE (P54865)
Analyse AlphaFold monomer V2.0 prediction for bifunctional XYLANASE/DEACETYLASE (P54865) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P54865
- Type
- protein
- Length
- 644 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x779f96120E362e0087Bcf74E47F0beFA4c1C62cd
- Molecule
- Bifunctional XYLANASE/DEACETYLASE
- UniProt
- P54865
- Pockets
- 6 · best druggability 0.53
Structure
1 distinct chain · 15% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bifunctional XYLANASE/DEACETYLASE | protein | 644 | 15% helix, 42% strand | P54865 |
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.53 | 0.76 | 37 | empty |
| 2 | 187 | 0.52 | 0.78 | 30 | empty |
| 3 | 151 | 0.42 | 0.75 | 23 | empty |
| 4 | 64 | 0.32 | 0.76 | 17 | empty |
| 5 | 71 | 0.29 | 0.73 | 20 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1E5B · Internal xylan binding domain from C. fimi XYN10A, R262G mutant · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1E5B · Internal xylan binding domain from C. fimi Xyn10A, R262G mutant · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 2XBD · Internal xylan binding domain from cellulomonas fimi xylanase D, NMR, minimized average… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 2XBD · Internal xylan binding domain from cellulomonas fimi xylanase D, NMR, minimized average… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1E5C · Internal xylan binding domain from C. fimi Xyn10A, R262G mutant · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1E5C · Internal xylan binding domain from C. fimi XYN10A, R262G mutant · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1XBD · Internal xylan binding domain from cellulomonas fimi xylanase D, NMR, 5 structures · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1XBD · Internal xylan binding domain from cellulomonas fimi xylanase D, NMR, 5 structures · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 1HEH · C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A · an experimental structure of the same protein · chain A against C, TM-score 0.13
- 1HEH · C-terminal xylan binding domain from cellulomonas fimi xylanase 11A · an experimental structure of the same protein · chain A against C, TM-score 0.13
- 1HEJ · C-terminal xylan binding domain from cellulomonas fimi xylanase 11A · an experimental structure of the same protein · chain A against C, TM-score 0.13
- 1HEJ · C-terminal xylan binding domain from Cellulomonas fimi xylanase 11A · an experimental structure of the same protein · chain A against C, TM-score 0.13
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 P54865
- Elsewhere: UniProt P54865 · AlphaFold DB P54865
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.