MolNFT v1 · #9106 · protein
X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9 ångströms resolution
1HLC · Human lectin: “X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with lactose at 2.9 ångströms…”. X-ray diffraction, 2 ligands (BGC, GAL), 2 pockets (best druggability 0.43). MolNFT v1 #9106 on…
- PDB
- 1HLC
- Type
- protein
- Length
- 258 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human lectin
- UniProt
- P05162
- Ligands
- BGC, GAL
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Human lectin | protein | 129 | 0% helix, 60% strand | P05162 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 119 | 0.43 | 0.77 | 17 | empty |
| 2 | 93 | 0.37 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 617 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
- 1HLC · X-ray crystal structure of the human dimeric S-lac lectin, L-14-II, in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P05162 · AlphaFold monomer V2.0 prediction for galectin-2 (P05162) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P05162
- Elsewhere: RCSB PDB 1HLC · PDBe 1HLC · UniProt P05162
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