MolNFT v1 · #1315 · protein
Erythrina corallodendron lectin
1AXY: “Erythrina corallodendron lectin”. X-ray diffraction, 7 ligands (NAG, MAN, BMA). MolNFT v1 #1315 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AXY
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lectin
- UniProt
- P16404
- Ligands
- NAG, MAN, BMA, XYP, FUC, MN, CA
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lectin | protein | 239 | 4% helix, 46% strand | P16404 |
Ligands and binding sites
- 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
- XYP · beta-D-xylopyranose · sugar
- FUC · alpha-L-fucopyranose · 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
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 1AXY · PDBe 1AXY · UniProt P16404
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