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Alkaline phosphatase

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Line 29: Line 29:
**[[2mlx]], [[2mly]], [[2mlz]] – EcALP + trigger factor<br />
**[[2mlx]], [[2mly]], [[2mlz]] – EcALP + trigger factor<br />
**[[1ali]], [[1ajb]], [[1ajc]], [[1ajd]], [[1alj]], [[1ani]], [[1anj]], [[2anh]], [[1hqa]], [[1urb]], [[1hjk]], [[1khk]], [[1kh7]] - EcALP (mutant) + Zn + Mg<br />
**[[1ali]], [[1ajb]], [[1ajc]], [[1ajd]], [[1alj]], [[1ani]], [[1anj]], [[2anh]], [[1hqa]], [[1urb]], [[1hjk]], [[1khk]], [[1kh7]] - EcALP (mutant) + Zn + Mg<br />
-
**[[1ura]] - EcALP (mutant) + Zn<br />
+
**[[1ura]], [[1khn]] , [[5tpq]] - EcALP (mutant) + Zn<br />
-
**[[1khn]] - EcALP (mutant) + Zn<br />
+
**[[1b8j]] - EcALP + Zn + Mg + VO4<br />
**[[1b8j]] - EcALP + Zn + Mg + VO4<br />
**[[5c66]] - EcALP + Zn + WO4<br />
**[[5c66]] - EcALP + Zn + WO4<br />
Line 72: Line 71:
**[[4kjg]] - rALP + Zn + Mg + nitrophenyl phosphate <br />
**[[4kjg]] - rALP + Zn + Mg + nitrophenyl phosphate <br />
**[[5jk4]] - ALP + phosphate - ''Stenotrophomonas maltophilia'' <br />
**[[5jk4]] - ALP + phosphate - ''Stenotrophomonas maltophilia'' <br />
-
**[[5tj3]] - ALP + Zn + phosphothreonine – ''Elizabethkingia meningoseptica''<br />
+
**[[5tj3]] - EmALP + Zn + phosphothreonine – ''Elizabethkingia meningoseptica''<br />
*ALP complexes
*ALP complexes
Line 78: Line 77:
**[[2mlx]], [[2mly]], [[2mlz]] - EcALP residues 220-310 + trigger factor - NMR<br />
**[[2mlx]], [[2mly]], [[2mlz]] - EcALP residues 220-310 + trigger factor - NMR<br />
**[[5jtl]] – EcALP + SecB<br />
**[[5jtl]] – EcALP + SecB<br />
 +
**[[5too]] - EmALP (mutant) + Zn <br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 11:19, 11 March 2018

E. coli alkaline phosphatase dimer with Zn+2 (grey), Mg+2 (green) and phosphate ions, 1elx

Drag the structure with the mouse to rotate

3D Structures of alkaline phosphatase

Updated on 11-March-2018

References

  1. ↑ Llinas P, Stura EA, Menez A, Kiss Z, Stigbrand T, Millan JL, Le Du MH. Structural studies of human placental alkaline phosphatase in complex with functional ligands. J Mol Biol. 2005 Jul 15;350(3):441-51. PMID:15946677 doi:http://dx.doi.org/10.1016/j.jmb.2005.04.068
  2. ↑ Stec B, Hehir MJ, Brennan C, Nolte M, Kantrowitz ER. Kinetic and X-ray structural studies of three mutant E. coli alkaline phosphatases: insights into the catalytic mechanism without the nucleophile Ser102. J Mol Biol. 1998 Apr 3;277(3):647-62. PMID:9533886 doi:10.1006/jmbi.1998.1635

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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