Research workbench
AlphaFold monomer V2.0 prediction for D-xylose-binding periplasmic protein (P37387)
Analyse AlphaFold monomer V2.0 prediction for D-xylose-binding periplasmic protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P37387
- Type
- protein
- Length
- 330 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x80D2ac0F5e3268bC5C1d28BBAA07E3169BB02b79
- Molecule
- D-xylose-binding periplasmic protein
- UniProt
- P37387
Structure
1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-xylose-binding periplasmic protein | protein | 330 | 40% helix, 20% strand | P37387 |
Compared structures
- 3MA0 · Closed liganded crystal structure of xylose binding protein from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 3MA0 · Closed liganded crystal structure of xylose binding protein from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.93
- 3M9X · Open liganded crystal structure of xylose binding protein from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 3M9X · Open liganded crystal structure of xylose binding protein from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.78
- 3M9W · Open ligand-free crystal structure of xylose binding protein from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.77
- 3M9W · Open ligand-free crystal structure of xylose binding protein from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.77
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 P37387
- Elsewhere: UniProt P37387 · AlphaFold DB P37387
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