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Structure of mouse galectin-3 crd point mutant (V160A) in complex with td-139 belonging to P121 space group.
Analyse Structure of mouse galectin-3 crd point mutant (V160A) in complex with td-139… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CXC
- Type
- protein
- Length
- 274 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P16110
- Ligands
- TD2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 137 | — | P16110 |
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 · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7CXC · Structure of mouse Galectin-3 CRD point mutant (V160A) in complex with TD-139 belonging… · the same entry in another collection · chain A against A, TM-score 1.00
- P16110 · AlphaFold monomer V2.0 prediction for galectin-3 (P16110) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P16110
- Elsewhere: RCSB PDB 7CXC · PDBe 7CXC · UniProt P16110
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