Research workbench
Lectin domain of lectinolysin complexed with lewis B antigen
Analyse Lectin domain of lectinolysin complexed with lewis B antigen in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LEK
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Platelet aggregation factor sm-hpaf
- UniProt
- Q2PHL4
- Ligands
- FUC, NDG, GAL, CA, NI
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Platelet aggregation factor sm-hpaf | protein | 141 | 8% helix, 45% strand | Q2PHL4 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
- NI · Nickel (II) ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3LEK · Lectin Domain of Lectinolysin complexed with Lewis B Antigen · the same entry in another collection · 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 Q2PHL4
- Elsewhere: RCSB PDB 3LEK · PDBe 3LEK · UniProt Q2PHL4
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