2ek9: Difference between revisions
New page: left|200px {{Structure |PDB= 2ek9 |SIZE=350|CAPTION= <scene name='initialview01'>2ek9</scene>, resolution 1.97Å |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+F... |
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|GENE= | |GENE= | ||
|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam04389 Peptidase_M28], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02133 PA_C5a_like]</span> | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam04389 Peptidase_M28], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=cd02133 PA_C5a_like]</span> | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ek9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek9 OCA], [http://www.ebi.ac.uk/pdbsum/2ek9 PDBsum | |RELATEDENTRY= | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ek9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ek9 OCA], [http://www.ebi.ac.uk/pdbsum/2ek9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ek9 RCSB]</span> | |||
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[[Category: metalloproteinase]] | [[Category: metalloproteinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:50:23 2008'' | ||
Revision as of 02:50, 31 March 2008
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| , resolution 1.97Å | |||||||
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| Sites: | , , , , , , and | ||||||
| Ligands: | , , | ||||||
| Domains: | Peptidase_M28, PA_C5a_like | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Aminopeptidase from Aneurinibacillus sp. strain AM-1 with Bestatin
OverviewOverview
To elucidate the structure and molecular mechanism of a characteristic proline-specific aminopeptidase produced by the thermophile Aneurinibacillus sp. strain AM-1, its gene was cloned and the recombinant protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 1.8 A resolution from the recombinant aminopeptidase crystal. The crystals belong to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 93.62, b = 68.20, c = 76.84 A. A complete data set was also obtained from crystals of SeMet-substituted aminopeptidase. Data in the resolution range 20-2.1 A from the MAD data set from the SeMet-substituted crystal were used for phase determination.
About this StructureAbout this Structure
2EK9 is a Single protein structure of sequence from Bacteria. Full crystallographic information is available from OCA.
ReferenceReference
Overexpression, purification, crystallization and preliminary X-ray crystallographic studies of a proline-specific aminopeptidase from Aneurinibacillus sp. strain AM-1., Akioka M, Nakano H, Horikiri A, Tsujimoto Y, Matsui H, Shimizu T, Nakatsu T, Kato H, Watanabe K, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt, 12):1266-8. Epub 2006 Nov 30. PMID:17142913
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