Research workbench
The rslex - sulfonato-CALIX[8]ARENE complex, P3 form, acetate pH 4.0
Analyse The rslex - sulfonato-CALIX[8]ARENE complex, P3 form, acetate pH 4.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ALG
- Type
- protein
- Length
- 180 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fucose-binding lectin protein
- UniProt
- A0A0S4TLR1
- Ligands
- BDF, EVB
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 67% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fucose-binding lectin protein | protein | 90 | 0% helix, 67% strand | A0A0S4TLR1 |
Ligands and binding sites
- BDF · beta-D-fructopyranose · ligand · 4 copies · chains A, B
- EVB · sulfonato-calix[8]arene · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7ALG · The RSLex - sulfonato-calix[8]arene complex, P3 form, acetate pH 4.0 · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A0S4TLR1
- Elsewhere: RCSB PDB 7ALG · PDBe 7ALG · UniProt A0A0S4TLR1
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