PDB ID or protein name

1le6 » Phospholipase A2, group X

1le6 » Phospholipase A2, group X
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Topology in Secreted
Topologyout side
in side
1le6 » Phospholipase A2, group X
Depth 7.4 ± 0.9 Å
Tilt Angle 78 ± 6°
ΔGtransfer -13.2 kcal/mol
Links to 1le6 PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology out
Resolution 1.9 Å
Other PDB entries representing this structure 1le7, 4uy1, 5g3m, 5g3n
Number of subunits 1
Experimental Verification for 1le6 » Phospholipase A2, group X
Calculated transfer energy is larger than a maximal experimental value (-6.1 kcal/mol, Bezzine et al. 2002). Perhaps the experimental data reflects the membrane-binding affinity of a premicellar protein-lipid aggregate (Pan et al. 2002); hence, the large exposed hydrophobic surface of the membrane-dissociated protein might be partially covered by lipid.
2 references
Bezzine, S., Bollinger, J.G., Singer, A.G., Veatch, S.L., Keller, S.L., and Gelb, M.H. 2002. On the binding preference of human groups IIA and X phospholipases A2 for membranes with anionic phospholipids. J Biol Chem. 277:48523-48534. PubMed
Pan YH, Yu BZ, Singer AG, Ghomashchi F, Lambeau G, Gelb MH, Jain MK, Bahnson BJ. 2002. Crystal structure of human group X secreted phospholipase A2. Electrostatically neutral interfacial surface targets zwitterionic membranes. J Biol Chem. 277:29086-93. PubMed
Comments on 1le6 » Phospholipase A2, group X
Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers uncharged phosphatidylethanolamine and phosphatidylcholine liposomes to those of charged phosphatidylserine (a unique feature of this phospholipase).