Research workbench
Crystal structure of human galectin-9 N-terminal crd in complex with N-acetyllactosamine dimer (crystal 1)
Analyse Crystal structure of human galectin-9 N-terminal crd in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZHK
- Type
- protein
- Length
- 283 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galectin-9
- UniProt
- O00182
- Ligands
- NAG, GAL
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galectin-9 | protein | 141 | 2% helix, 54% strand | O00182 |
| B | Galectin-9 | protein | 142 | 2% helix, 54% strand | O00182 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 238 | 0.49 | 0.75 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 237 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 2ZHK · Crystal structure of human galectin-9 N-terminal CRD in complex with N-acetyllactosamine… · the same entry in another collection · chain A against A, TM-score 1.00
- O00182 · AlphaFold monomer V2.0 prediction for galectin-9 (O00182) · a predicted model of the same protein · chain B 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 O00182
- Elsewhere: RCSB PDB 2ZHK · PDBe 2ZHK · UniProt O00182
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