1mc2
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1mc2 |SIZE=350|CAPTION= <scene name='initialview01'>1mc2</scene>, resolution 0.85Å | |PDB= 1mc2 |SIZE=350|CAPTION= <scene name='initialview01'>1mc2</scene>, resolution 0.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL ALCOHOL'>IPA</scene> | + | |LIGAND= <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mc2 OCA], [http://www.ebi.ac.uk/pdbsum/1mc2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mc2 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Weeks, C M.]] | [[Category: Weeks, C M.]] | ||
[[Category: Zhang, R G.]] | [[Category: Zhang, R G.]] | ||
| - | [[Category: IPA]] | ||
[[Category: agkistrodon acutus]] | [[Category: agkistrodon acutus]] | ||
[[Category: snake venom]] | [[Category: snake venom]] | ||
[[Category: ys49-phospholipase a2]] | [[Category: ys49-phospholipase a2]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:14:11 2008'' |
Revision as of 19:14, 30 March 2008
| |||||||
| , resolution 0.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
monomeric LYS-49 phospholipase A2 homologue purified from AG
Overview
The crystal structure of acutohaemolysin, a lysine 49 phospholipase A2 protein with 1010 non-hydrogen protein atoms and 232 water molecules, has been determined ab initio using the program SnB at an ultrahigh resolution of 0.8 A. The lack of catalytic activity appears to be related to the presence of Phe102, which prevents the access of substrate to the active site. The substitution of tryptophan for leucine at residue 10 interferes with dimer formation and may be responsible for the additional loss of hemolytic activity. The ultrahigh resolution of the experimental diffraction data permits alternative conformations to be modeled for disordered residues, many hydrogen atoms to be located, the protonation of the Nepsilon2 atom in the catalytic residue His48 to be observed experimentally, and the density of the bonding electrons to be analyzed in detail.
About this Structure
1MC2 is a Single protein structure of sequence from Deinagkistrodon acutus. Full crystallographic information is available from OCA.
Reference
The crystal structure of a novel, inactive, lysine 49 PLA2 from Agkistrodon acutus venom: an ultrahigh resolution, AB initio structure determination., Liu Q, Huang Q, Teng M, Weeks CM, Jelsch C, Zhang R, Niu L, J Biol Chem. 2003 Oct 17;278(42):41400-8. Epub 2003 Jul 19. PMID:12871974
Page seeded by OCA on Sun Mar 30 22:14:11 2008
