1VL9: Atomic Resolution (0.97a) Structure Of The Triple Mutant (k53,56,121m) Of Bovine Pancreatic Phospholipase A2

Citation:
Abstract
The enzyme phospholipase A2 catalyzes the hydrolysis of the sn-2 acyl chain of phospholipids, forming fatty acids and lysophospholipids. The crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 A). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47 degrees. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% (Rfree = 13.4%) using 63,926 unique reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are ordered and have clear electron density.
PDB ID: 1VL9Download
MMDB ID: 30076
PDB Deposition Date: 2004/7/15
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 0.97  Å
Source Organism:
Similar Structures:
Biological Unit for 1VL9: monomeric; determined by author
Molecular Components in 1VL9
Label Count Molecule
Protein (1 molecule)
1
Phospholipase A2(Gene symbol: PLA2G1B)
Molecule annotation
Chemicals (9 molecules)
1
2
2
1
3
3
4
3
* Click molecule labels to explore molecular sequence information.

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