Crystal structure of porcine pancreatic phospholipase A₂ in complex with 2-methoxycyclohexa-2-5-diene-1,4-dione

Figures & data

Table 1. Data collection and refinement statistics of PLA₂–MCW complex crystal.

Data collection statistics
Space group
Cell dimensions (Å)
a=b	68.36
c	70.12
Matthews coefficient (V m) ()	3.38
Solvent content (%)	63.61
Resolution range (Å)	45.24–2.50
Highest resolution shell (Å)	2.64–2.50
Total number of reflections	18838
Number of unique reflections	6811
Overall completeness (%)	97.3
Completeness in the highest resolution shell	91.3
R merge (%)	7.3
Mean overall I/σ	22.5
Ł Refinement statistics
Resolutions limits (Å)	13.65–2.50
Number of reflections	6759
R factor (%)	18.0
R free (%)	22.9
Number of protein atoms	972
Number of ligand atoms	10
Number of calcium ions	2
Number of water molecules	32
RMS deviations from ideal values
Bond lengths (Å)	0.020
Bond angles (deg)	1.905
Dihedral angles (deg)	20.395
Average B factor (Å^2)	22.69

Figure 1. Chemical structures of (a) MCW and (b) curcumin.

Figure 2. Electron density map of MCW bound at the active site of PLA₂. Dashed lines indicate three water-mediated hydrogen bonds with residues of Arg 6, Cys 23 and Gly 30 of the enzyme.

Figure 3. The best docked pose of curcumin at the active site of PLA₂. Dashed lines indicate hydrogen bonds.

Figure 4. Relative positions and orientation of MCW (blue) and curcumin (pink) at the active site of PLA₂.