1bsg: Difference between revisions
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|PDB= 1bsg |SIZE=350|CAPTION= <scene name='initialview01'>1bsg</scene>, resolution 1.85Å | |PDB= 1bsg |SIZE=350|CAPTION= <scene name='initialview01'>1bsg</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsg OCA], [http://www.ebi.ac.uk/pdbsum/1bsg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bsg RCSB]</span> | |||
}} | }} | ||
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[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
[[Category: Fonze, E.]] | [[Category: Fonze, E.]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: penicillin]] | [[Category: penicillin]] | ||
''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 19:07:19 2008'' | ||
Revision as of 19:07, 30 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-LACTAMASE FROM STREPTOMYCES ALBUS G
OverviewOverview
The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.
About this StructureAbout this Structure
1BSG is a Single protein structure of sequence from Streptomyces albus g. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution., Dideberg O, Charlier P, Wery JP, Dehottay P, Dusart J, Erpicum T, Frere JM, Ghuysen JM, Biochem J. 1987 Aug 1;245(3):911-3. PMID:3499147
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