Research workbench
Structure of helix aspersa agglutinin with natural glycosylation and N-acetyl-alpha-D-galactosamine (galnac)
Analyse Structure of helix aspersa agglutinin with natural glycosylation and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Q56
- Type
- protein
- Length
- 101 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Helix aspersa agglutinin (haa)
- Ligands
- NAG, FUC, GAL, BMA, A2G, NA, ZN
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Helix aspersa agglutinin (haa) | protein | 101 | 3% helix, 53% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- FUC · alpha-L-fucopyranose · sugar · 2 copies · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- BMA · beta-D-mannopyranose · sugar
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
- NA · Sodium ion · metal · chains A
- ZN · Zinc ion · metal · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, cyclization).
Compared structures
- 4Q56 · Structure of Helix aspersa agglutinin with natural glycosylation and… · 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 4Q56 · PDBe 4Q56
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