Functionally selective inhibition of group iia phospholipase A2 reveals a role for vimentin in regulating arachidonic acid metabolism

Structure

x-ray diffraction · 1 distinct chain · 48% helix, 6% strand (DSSP).

Ligands and binding sites

• U8D · (3-{[3-(2-amino-2-oxoethyl)-1-benzyl-2-ethyl-1H-indol-5-yl]oxy}propyl)phosphonic acid · ligand · 2 copies · chains A, B
• CA · Calcium ion · metal · 4 copies · chains A, B
• CL · Chloride ion · ion · 4 copies · 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 · 639 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 14 disulfide (disulfide).

Compared structures

• 3U8D · Functionally selective inhibition of Group IIA phospholipase A2 reveals a role for… · the same entry in another collection · chain A against A, TM-score 1.00
• P14555 · AlphaFold monomer V2.0 prediction for phospholipase A2, membrane associated (P14555) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P14555
• Elsewhere: RCSB PDB 3U8D · PDBe 3U8D · UniProt P14555