Crystal structure of FK506-binding protein 1A from aspergillus fumigatus bound to ascomycin

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 39% strand (DSSP).

Ligands and binding sites

• KXX · (3s,4r,5s,8r,9e,12s,14s,15r,16s,18r,19r,22r,26as)-8-ethyl-5,19-dihydroxy-3-{(1E)-1-[(1R,3R,4R)-4-hydroxy-3-methoxycyclohexyl]prop-1-en-2-yl}-14,16-dimethoxy-4, 10,12,18-tetramethyl-5,6,8,11,12,13,14,15,16,17,18,19, 24,25,26,26A-hexadecahydro-3H-15,19-epoxypyrido[2,1-c][1,4]oxazacyclotricosine-1,7,20,21(4H,23H)-tetrone · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 2 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · 3 copies · chains A, B
• P6G · Hexaethylene glycol · additive · chains A
• ACT · Acetate ion · additive · chains A
• 1PE · Pentaethylene glycol · additive · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 69 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 7U0S · Crystal Structure of FK506-binding protein 1A from Aspergillus fumigatus Bound to… · the same entry in another collection · chain A against A, TM-score 1.00
• Q4WLV6 · AlphaFold monomer V2.0 prediction for FK506-binding protein 1A (Q4WLV6) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 Q4WLV6
• Elsewhere: RCSB PDB 7U0S · PDBe 7U0S · UniProt Q4WLV6