Structure of a phosphatidylinositol-phosphate synthase (pips) from mycobacterium kansasii with evidence of substrate binding

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 13% strand (DSSP).

Ligands and binding sites

• 8K6 · Octadecane · ligand · 6 copies · chains A, C
• LIP · L-myo-inositol-1-phosphate · ligand · chains A, C
• TCE · 3,3',3''-phosphanetriyltripropanoic acid · ligand · chains A
• C5P · Cytidine-5'-monophosphate · ligand · chains C
• NA · Sodium ion · metal · 4 copies · chains A, C
• OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 7 copies · chains A, C
• GOL · Glycerol · additive · 3 copies · chains A, C
• 1PE · Pentaethylene glycol · additive · 2 copies · chains A, C
• FLC · Citrate anion · additive · chains A, C

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

Pockets

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

Interfaces

1 interface between chains.

• A–C · 2309 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

• 6WMV · Structure of a phosphatidylinositol-phosphate synthase (PIPS) from Mycobacterium kansasii… · 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 A0A101DFK9
• Every structure of UniProt U5WZP7
• Elsewhere: RCSB PDB 6WMV · PDBe 6WMV · UniProt A0A101DFK9 · UniProt U5WZP7