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Crystal structure of human galectin-3 crd in complex with 3- fluophenyl-1,2,3-triazolyl thiodigalactoside inhibitor
Analyse Crystal structure of human galectin-3 crd in complex with 3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5E89
- Type
- protein
- Length
- 137 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galectin-3
- UniProt
- P17931
- Ligands
- TD2, CL
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galectin-3 | protein | 137 | 2% helix, 62% strand | P17931 |
Ligands and binding sites
- TD2 · 3-deoxy-3-[4-(3-fluorophenyl)-1H-1,2,3-triazol-1-yl]-beta-D-galactopyranosyl 3-deoxy-3-[4-(3-fluorophenyl)-1H-1,2,3-triazol-1-yl]-1-thio-beta-D-galactopyranoside · ligand · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5E89 · Crystal structure of Human galectin-3 CRD in complex with 3-fluophenyl-1,2,3-triazolyl… · 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 P17931
- Elsewhere: RCSB PDB 5E89 · PDBe 5E89 · UniProt P17931
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