Research workbench
CGL2 in complex with blood group H type II
Analyse CGL2 in complex with blood group H type II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ULD
- Type
- protein
- Length
- 600 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galectin-2
- Ligands
- NAG, GAL, FUC
- Pockets
- 5 · best druggability 0.55
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Galectin-2 | protein | 150 | 0% helix, 49% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, D, B, C
- GAL · beta-D-galactopyranose · sugar · 4 copies · chains A, B, C, D
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, D, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 159 | 0.55 | 0.81 | 31 | empty |
| 2 | 126 | 0.50 | 0.81 | 22 | empty |
| 3 | 115 | 0.49 | 0.80 | 19 | empty |
| 4 | 116 | 0.48 | 0.80 | 20 | empty |
| 5 | 212 | 0.46 | 0.74 | 24 | empty |
Interfaces
4 interfaces between chains.
- A–B · 983 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 981 Ų buried · 15 hydrogen bonds · protein-protein
- A–D · 238 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 17 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ULD · CGL2 in complex with blood group H type II · the same entry in another collection · chain B against B, 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
- Elsewhere: RCSB PDB 1ULD · PDBe 1ULD
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