Human afamin orthorhombic crystal form by controlled hydration

Structure

x-ray diffraction · 1 distinct chain.

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
• NA · Sodium ion · metal · chains A
• CL · Chloride ion · ion · chains A
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A
• P6G · Hexaethylene glycol · additive · 2 copies · chains A
• PG4 · Tetraethylene glycol · additive · 2 copies · chains A
• PGE · Triethylene glycol · additive · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · 2 copies · chains A
• ACT · Acetate ion · additive · chains A
• PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

• 6FAK · Human afamin orthorhombic crystal form by controlled hydration · the same entry in another collection · chain A against A, TM-score 1.00
• P43652 · AlphaFold monomer V2.0 prediction for afamin (P43652) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P43652
• Elsewhere: RCSB PDB 6FAK · PDBe 6FAK · UniProt P43652