Research workbench
Cg-16, a homodimeric agglutinin from chicken liver
Analyse Cg-16, a homodimeric agglutinin from chicken liver in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QMJ
- Type
- protein
- Length
- 264 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactoside-binding lectin
- UniProt
- P23668
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Beta-galactoside-binding lectin | protein | 132 | 0% helix, 60% strand | P23668 |
Ligands and binding sites
- BME · Beta-mercaptoethanol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 591 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent (additive adduct).
Compared structures
- 1QMJ · CG-16, a homodimeric agglutinin from chicken liver · the same entry in another collection · chain A against A, TM-score 1.00
- P23668 · AlphaFold monomer V2.0 prediction for 16 kda beta-galactoside-binding lectin (P23668) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P23668
- Elsewhere: RCSB PDB 1QMJ · PDBe 1QMJ · UniProt P23668
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