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Uda tetrasaccharide complex. crystal structure of urtica dioica agglutinin, a superantigen presented by MHC molecules of class I and class II
Analyse Uda tetrasaccharide complex. crystal structure of urtica dioica agglutinin, a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EN2
- Type
- protein
- Length
- 86 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Agglutinin isolectin I/AGGLUTININ isolectin V/ agglutinin isolectin VI
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Agglutinin isolectin I/AGGLUTININ isolectin V/ agglutinin isolectin VI | protein | 86 | 23% helix, 23% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 8 disulfide, 1 modified (disulfide, cyclization).
Compared structures
- 1EN2 · Uda tetrasaccharide complex. crystal structure of urtica dioica agglutinin, a… · 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
- Elsewhere: RCSB PDB 1EN2 · PDBe 1EN2
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