2aut
Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium
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| , resolution 2.25Å | |||||||
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| Ligands: | , , | ||||||
| Gene: | aphA (Salmonella typhimurium) | ||||||
| Activity: | Acid phosphatase, with EC number 3.1.3.2 | ||||||
| Related: | 1Z5G, 1Z5U, 1Z88
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
The aphA gene of Salmonella enterica sv. Typhimurium strain MD6001 was cloned in the multicopy plasmid pBluescript SK(-). The recombinant AphA protein was purified to homogeneity. The protein crystallized in the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 112.4, b = 130.2, c = 139.6 A. Consistent with the self-rotation function, there are two tetramers in the asymmetric unit, indicating a solvent content of approximately 54%. The crystals are composed of biologically active AphA molecules.
About this StructureAbout this Structure
2AUT is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
ReferenceReference
Expression, purification, crystallization and preliminary X-ray diffraction studies of recombinant class B non-specific acid phosphatase of Salmonella typhimurium., Makde RD, Kumar V, Gupta GD, Jasti J, Singh TP, Mahajan SK, Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1849-52. Epub 2003, Sep 19. PMID:14501135
Page seeded by OCA on Mon Mar 31 01:57:38 2008