MolNFT v1 · #13959 · protein
Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose
1LTE · Coral tree lectin: “Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose”. X-ray diffraction, 9 ligands (XYL, NAG, MAN). MolNFT v1 #13959 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1LTE
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Coral tree lectin
- UniProt
- P16404
- Ligands
- XYL, NAG, MAN, BMA, FUC, BGC, GAL, MN, CA
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Coral tree lectin | protein | 239 | 4% helix, 45% strand | P16404 |
Ligands and binding sites
- XYL · Xylitol · ligand
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- BMA · beta-D-mannopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A
- BGC · beta-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- MN · Manganese (II) ion · metal · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 glycan (N-glycosylation).
Compared structures
- 1LTE · Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose · the same entry in another collection · chain A against A, TM-score 1.00
- P16404 · AlphaFold monomer V2.0 prediction for lectin (P16404) · a predicted model of the same protein · 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 P16404
- Elsewhere: RCSB PDB 1LTE · PDBe 1LTE · UniProt P16404
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