Research workbench
Metal-free (apo) P. angolensis seed lectin in complex with man- ALPHA(1-3)MAN-ALPHA(1-6)MAN
Analyse Metal-free (apo) P. angolensis seed lectin in complex with man… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GN7
- Type
- protein
- Length
- 457 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lectin
- UniProt
- Q8GSD2
- Ligands
- MAN, BMA
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lectin | protein | 225 | 3% helix, 50% strand | Q8GSD2 |
| B | Lectin | protein | 232 | 4% helix, 46% strand | Q8GSD2 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 902 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (cyclization).
Compared structures
- 2GN7 · Metal-free (apo) P. angolensis seed lectin in complex with Man-alpha(1-3)Man-alpha(1-6)Man · 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 Q8GSD2
- Elsewhere: RCSB PDB 2GN7 · PDBe 2GN7 · UniProt Q8GSD2
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